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Information on EC 3.1.3.1 - alkaline phosphatase
for references in articles please use BRENDA:EC3.1.3.1
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.1 alkaline phosphatase
IUBMB Comments
Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase)
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
- 3.1.3.1
- osteoblast
- osteocalcin
-
osteogenic
- collagen
- aminotransferase
- bilirubin
- women
- mesenchymal
- albumin
- pancreatitis
- marrow
- parathyroid
- phosphorus
- urinary
- cholesterol
- osteoporosis
- creatinine
- resorption
- arterial
- fracture
- children
-
alt
- necrosis
- pain
- femoral
- spine
- transaminase
-
osteogenesis
-
lumbar
- biliary
-
morphogenetic
- osteopontin
- anterior
- bile
- femur
- periodontal
-
radiological
-
gamma-glutamyl
- calcification
- dental
-
postoperative
-
biocompatibility
- gg
-
preoperative
- transpeptidase
- ligament
-
admission
-
postmenopausal
- trabecular
-
hepatoprotective
- biotechnology
- agriculture
- medicine
- food industry
- environmental protection
- analysis
- molecular biology
- diagnostics
- synthesis
showSynonyms
ap, alkaline phosphatase, bone alkaline phosphatase, placental alkaline phosphatase, alpase, apase, intestinal alkaline phosphatase, tnsalp, phosphomonoesterase, secreted alkaline phosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkaline p-nitrophenylphosphate phosphatase
alkaline phenyl phosphatase
-
-
-
-
alkaline phosphatase
alkaline phosphatase 4
alkaline phosphatase IV
alkaline phosphatase, tissue-nonspecific isozyme
alkaline phosphohydrolase
-
-
-
-
alkaline phosphomonoesterase
-
-
-
-
ALP
ALPase
ALPI
ALPL
alr5291
-
alr5291 encodes a protein that is an atypical alkaline phosphatase like other cyanobacteria PhoAs
AP
AP-TNAP
-
-
-
-
AP3
APase
APASED
-
-
-
-
BC6
-
-
-
-
CAPase
CIAP
EAP
-
-
-
-
Germ-cell alkaline phosphatase
-
-
-
-
glycerophosphatase
-
-
-
-
H-AP
HaALP
High molecular weight phosphatase
-
-
-
-
IAP
IAPase
intestinal alkaline phosphatase
intestinal-type alkaline phosphatase
L-AP
Liver/bone/kidney isozyme
-
-
-
-
Low molecular weight phosphatase
-
-
-
-
M-ALP
-
-
-
-
Nagao isozyme
-
-
-
-
non-specific alkaline phosphatase
-
-
-
-
OE5192R
PHOA
phoK
phosphatase, alkaline
-
-
-
-
phosphomonoesterase
-
-
-
-
phox
PLAP
PLAP-like
-
-
-
-
RAN1
-
-
-
-
Regan isozyme
-
-
-
-
SAP
tissue non-specific alkaline phosphatase
tissue-nonspecific alkaline phosphatase
TNAP
TNSALP
ALP
-
-
-
-
APase
-
-
-
-
H-AP
-
-
-
-
IAP
-
-
-
-
L-AP
-
-
-
-
tissue-nonspecific alkaline phosphatase
-
-
TNSALP
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phosphate monoester + H2O = an alcohol + phosphate
double in-line displacement mechanism involving two-metal ion catalysis
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, catalytically active His153 and His328
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, active site structure, highly conserved in evolution of alkaline phosphatases
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, active site structure, mechanism
shrimp
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, substrate binding and active site structure
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Arg166 contributes to catalysis through binding interactions and through additional transition state stabilization that may arise from complementarity of the guanidinum group to the geometry of the trigonal bipyramidal transition state
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
phosphomonoester
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
diethylphosphate degradation
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SYSTEMATIC NAME
IUBMB Comments
phosphate-monoester phosphohydrolase (alkaline optimum)
Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase)
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CAS REGISTRY NUMBER
COMMENTARY
9001-78-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosine 5'-monophosphate + H2O
?
Substrates: 113.3% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
2'-[2-benzthiazole]-6'-hydroxybenzthiazole phosphate + H2O
2'-[2-benzthiazole]-6'-hydroxybenzthiazole + phosphate
-
Substrates: weakly fluorescent substrate
Products: highly fluorescent product
Products: highly fluorescent product
?
2,4-dinitrophenyl phosphate + H2O
2,4-dinitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate + H2O
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenol + phosphate
-
Substrates: CDP-star
Products: -
Products: -
?
2-chloro-5-(4-methoxyspiro[1,2-dioxetane-3,2'-(5-chloro)tricyclo[3.3.1.13.7]decan)-4-yl]-1-phenyl phosphate + H2O
2-chloro-5-(4-methoxyspiro[1,2-dioxetane-3,2'-(5-chloro)tricyclo[3.3.1.13.7]decan)-4-yl]-1-phenol + phosphate
2-glycerol phosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
Products: -
?
2-naphtyl phosphate + H2O
2-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
3'-ITP + H2O
?
-
Substrates: 51.5% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
3-nitrobenzyl phosphate + H2O
3-nitrobenzoate + phosphate
Substrates: -
Products: -
Products: -
?
3-nitrophenyl phosphate + H2O
3-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-aminophenyl phosphate + H2O
4-aminophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-hydroxybutyl phosphate + H2O
4-hydroxybutanol + phosphate
Substrates: -
Products: -
Products: -
?
4-methoxy-4-(3-phosphatephenyl)spiro [1,2-dioxetane-3,2'-adamantane] disodium salt + H2O
?
Substrates: -
Products: -
Products: -
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
Substrates: -
Products: -
Products: -
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
Substrates: 80% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
5-bromo-4-chloro-3-indolyl phosphate + H2O
5-bromo-4-chloro-indole + phosphate
Thermus sp. NTU-237
A0A1B2YKT4
Substrates: -
Products: -
Products: -
?
5-bromo-4-chloro-3-indolyl phosphate + nitroblue tetrazolium
?
-
Substrates: i.e. BCIP/NBT system
Products: -
Products: -
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
acscorbic acid-2-phosphate + H2O
ascorbate + phosphate
Substrates: -
Products: -
Products: -
?
adenosine 5'-(beta-glucosyl)diphosphate + H2O
?
-
Substrates: 29.8% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
adenosine 5'-diphosphate + H2O
AMP + phosphate
-
Substrates: 77% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
adenosine 5'-triphosphate + H2O
?
Substrates: 257.4% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
adenosine 5'-triphosphate + H2O
AMP + phosphate
-
Substrates: 61% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
alpha-naphthyl acid phosphate + H2O
?
Substrates: 88.6% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
beta-glycerol phosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
beta-glycerophosphate + H2O
? + phosphate
A0A196MRA0
Substrates: 33.2% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
bis(p-nitrophenyl) phosphate + H2O
?
Substrates: 6.1% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
bis-4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
cysteamine S-phosphate + H2O
cysteamine + phosphate
-
Substrates: -
Products: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: 52% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
D-glucose-1-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
Products: -
?
dATP + H2O
dADP + phosphate
A0A196MRA0
Substrates: 35.1% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
dCTP + H2O
dCDP + phosphate
A0A196MRA0
Substrates: 38.2% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
dGTP + H2O
dGDP + phosphate
A0A196MRA0
Substrates: 49.8% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
disodium 3-(4-meth- oxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]- decan]-4-yl)phenyl phosphate + H2O
?
Substrates: -
Products: -
Products: -
?
dTTP + H2O
dTDP + phosphate
A0A196MRA0
Substrates: 47.8% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
ethyl phosphate + H2O
ethanol + phosphate
Substrates: -
Products: -
Products: -
?
gamma-glycerophosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
glycerol 3-phosphate + H2O
glycerol + phosphate
A0A196MRA0
Substrates: 13.1% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
glycerol-1-phosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
Products: -
?
glycerol-2-phosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
Products: -
?
glycerophosphate + H2O
?
Substrates: 248.7% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
histone II-A + H2O
?
-
Substrates: enzyme shows protein phosphatase activity
Products: -
Products: -
?
indoxyl phosphate + nitroblue tetrazolium chloride
nitrioblue diformazan + phosphate
-
Substrates: -
Products: -
Products: -
?
inosine-5'-monophosphate + H2O
inosine + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
lipopolysaccharide + H2O
? + phosphate
Substrates: substrate is Escherichia coli B lipopolysaccharide
Products: -
Products: -
?
methyl 3-nitrophenyl phosphate + H2O
methyl phosphate + 3-nitrophenol
Substrates: -
Products: -
Products: -
?
methyl 4-nitrophenyl phosphate + H2O
methyl phosphate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
methyl 4-nitrophenyl phosphorothioate + H2O
4-nitrophenol + methyl phosphorothioate
Substrates: only the R-enantiomer is detectably hydrolyzed by the enzyme
Products: -
Products: -
?
methyl p-nitrophenyl phosphate + H2O
methanol + p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
methyl p-nitrophenyl phosphorothioate + H2O
methanol + p-nitrophenol + phosphorothioate
-
Substrates: -
Products: -
Products: -
?
methylphenyl phosphate + H2O
methyl phosphate + phenol
Substrates: -
Products: -
Products: -
?
N-acetylcysteamine S-phosphate + H2O
N-acetylcysteamine + phosphate
-
Substrates: -
Products: -
Products: -
?
NADP+ + H2O
?
-
Substrates: 20% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
o-carboxyphenyl phosphate + H2O
o-carboxyphenol + phosphate
-
Substrates: -
Products: -
Products: -
?
O-phospho-DL-serine + H2O
DL-serine + phosphate
-
Substrates: -
Products: -
Products: -
?
O-phospho-DL-tyrosine + H2O
DL-tyrosine + phosphate
-
Substrates: -
Products: -
Products: -
?
O-phosphoethanolamine + H2O
ethanolamine + phosphate
Substrates: -
Products: -
Products: -
?
p-toluidinium 5-bromo-4-chloro-3-indolyl phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
Substrates: -
Products: -
Products: -
?
phospho-Tyr angiotensin + H2O
angiotensin + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphothreonine + H2O
phosphate + Thr
-
Substrates: 22.1% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
phosphotyrosine + H2O
phosphate + Tyr
-
Substrates: 23.7% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
phytic acid + H2O
myo-inositol pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
propargyl phosphate + H2O
prop-1-yne + phosphate
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
riboflavin 5'-phosphate + H2O
riboflavin + phosphate
-
Substrates: -
Products: -
Products: -
?
S-[2-(methoxy carbonyl)ethyl] phosphorothioate + H2O
?
-
Substrates: -
Products: -
Products: -
?
thiamin diphosphate + H2O
thiamin phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + H2O
?
-
Substrates: 20% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
uridine 5'-monophosphate + H2O
?
Substrates: 388.6% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
[(4-chlorophenyl)thio](10-methyl-9(10H)-acridinylidene)-methanol 1-(dihydrogenphosphate) disodium salt + H2O
?
Substrates: -
Products: -
Products: -
?
2',3-AMP + H2O
?
-
Substrates: 20% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
2',3-AMP + H2O
?
-
Substrates: 20% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
2-chloro-5-(4-methoxyspiro[1,2-dioxetane-3,2'-(5-chloro)tricyclo[3.3.1.13.7]decan)-4-yl]-1-phenyl phosphate + H2O
2-chloro-5-(4-methoxyspiro[1,2-dioxetane-3,2'-(5-chloro)tricyclo[3.3.1.13.7]decan)-4-yl]-1-phenol + phosphate
Substrates: i.e. CDP-Star, chemoluminescent substrate
Products: -
Products: -
?
2-chloro-5-(4-methoxyspiro[1,2-dioxetane-3,2'-(5-chloro)tricyclo[3.3.1.13.7]decan)-4-yl]-1-phenyl phosphate + H2O
2-chloro-5-(4-methoxyspiro[1,2-dioxetane-3,2'-(5-chloro)tricyclo[3.3.1.13.7]decan)-4-yl]-1-phenol + phosphate
Substrates: i.e. CDP-Star , chemoluminescent substrate
Products: -
Products: -
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: 53.7% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: hydrolyzed by isoenzyme III, weak activity with isoenzyme I and II
Products: -
Products: -
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: wild-type activity is 16.9% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 16.3fold higher than activity from wild-type enzyme
Products: -
Products: -
?
3'-AMP + H2O
adenosine + phosphate
-
Substrates: -
Products: -
Products: -
?
3'-AMP + H2O
adenosine + phosphate
-
Substrates: -
Products: -
Products: -
?
3-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: hydrolyzed by isoenzyme III, weak activity with isoenzyme II, no activity with isoenzyme I
Products: -
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3-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
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3-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
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3-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
3-phosphoglycerate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + H2O
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + H2O
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Bacillus licheniformis MTCC 1483
Substrates: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Bacillus sp. OK-1
-
Substrates: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: reaction is at least partially diffusion-controlled
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: non-specific, phosphoseryl intermediate
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: strong support for a model in which electrostatic interactions between the bimetallo Zn2+ site and a nonbridging phosphate ester oxygen atom make a significant contribution to the large rate enhancement observed for alkaline phosphatase-catalyzed phosphate monoester hydrolysis
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: hydrolysis of 4-nitrophenylphosphate is nonlinear with time when the enzyme is microinjected into reversed micelles (of hexadecyltrimethylammoniumbromide in cyclohexane, with 1-butanol as cosurfactant) that contain substrate
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: hydrolysis of 4-nitrophenylphosphate is nonlinear with time when the enzyme is microinjected into reversed micelles (of hexadecyltrimethylammoniumbromide in cyclohexane, with 1-butanol as cosurfactant) that contain substrate
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: allosteric mechanism
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: activity with mutant os-1 enzyme is 12.2fold higher than activity from wild-type enzyme
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: strongest affinity substrate
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: best substrate
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
A0A196MRA0
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: non-specific, via phosphoseryl intermediate
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Thermus sp. NTU-237
A0A1B2YKT4
Substrates: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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5'-AMP + H2O
adenosine + phosphate
-
Substrates: -
Products: -
Products: -
?
5'-AMP + H2O
adenosine + phosphate
-
Substrates: 90% of activity with p-nitrophenyl phosphate
Products: -
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5'-AMP + H2O
adenosine + phosphate
-
Substrates: 90% of activity with p-nitrophenyl phosphate
Products: -
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5'-AMP + H2O
adenosine + phosphate
-
Substrates: -
Products: -
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5'-CMP + H2O
cytidine + phosphate
-
Substrates: 80% of activity with p-nitrophenyl phosphate
Products: -
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5'-GMP + H2O
guanosine + phosphate
-
Substrates: 40% of activity with p-nitrophenyl phosphate
Products: -
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5'-UMP + H2O
uridine + phosphate
-
Substrates: 30% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
5-bromo-4-chloro-3-indolyl phosphate + H2O
?
Substrates: 50.3% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
5-bromo-4-chloro-3-indolyl phosphate + H2O
?
Substrates: 50.3% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
Substrates: -
Products: -
Products: -
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
Substrates: -
Products: -
Products: -
?
adenosine 5'-monophosphate + H2O
?
Substrates: 306.1% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
adenosine 5'-monophosphate + H2O
?
Substrates: 306.1% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
ADP + H2O
?
-
Substrates: 20% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
ADP + H2O
?
-
Substrates: 20% of activity with p-nitrophenyl phosphate
Products: -
Products: -
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ADP + H2O
AMP + phosphate
-
Substrates: wild-type activity is 16.9% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 1.2fold lower than activity from wild-type enzyme
Products: -
Products: -
?
ADP + H2O
AMP + phosphate
A0A196MRA0
Substrates: 57.0% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
alpha-glycerol phosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
Products: -
?
alpha-glycerol phosphate + H2O
glycerol + phosphate
Bacillus licheniformis MTCC 1483
Substrates: -
Products: -
Products: -
?
alpha-glycerophosphate + H2O
glycerol + phosphate
-
Substrates: 60% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
alpha-glycerophosphate + H2O
glycerol + phosphate
-
Substrates: low activity with alpha-isomer
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: hydrolyzed by isoenzyme II and III, no activity with isoenzyme I
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
Substrates: -
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
AMP + H2O
adenosine + phosphate
-
Substrates: alkaline phosphatase F I
Products: -
Products: -
?
AMP + H2O
adenosine + phosphate
-
Substrates: alkaline phosphatase F II
Products: -
Products: -
?
AMP + H2O
adenosine + phosphate
-
Substrates: wild-type activity is 9.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 18.2fold higher than activity from wild-type enzyme
Products: -
Products: -
?
AMP + H2O
adenosine + phosphate
Substrates: -
Products: -
Products: -
?
AMP + H2O
adenosine + phosphate
A0A196MRA0
Substrates: 39.3% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
ATP + H2O
?
-
Substrates: 57.8% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
ATP + H2O
?
-
Substrates: 10% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
ATP + H2O
?
-
Substrates: 10% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
ATP + H2O
?
-
Substrates: wild-type activity is 15.4% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 6.9fold higher than activity from wild-type enzyme
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
A0A196MRA0
Substrates: 70.6% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
Substrates: 20% of activity with p-nitrophenyl phosphate
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
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beta-glycerophosphate + H2O
glycerol + phosphate
Substrates: uranium precipitation assay: uranyl carbonate solution in carbonate-bicarbonate buffer, supplemented with beta-glycerophosphate as the substrate at 30°C under static nongrowing conditions in a final volume of 5 ml
Products: -
Products: -
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beta-glyceryl phosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
beta-glyceryl phosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
bis-p-nitrophenyl phosphate + H2O
?
-
Substrates: weak activity
Products: -
Products: -
?
casein + H2O
?
-
Substrates: enzyme shows protein phosphatase activity
Products: -
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?
casein + H2O
?
-
Substrates: enzyme shows protein phosphatase activity
Products: -
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?
CMP + H2O
cytidine + phosphate
-
Substrates: alkaline phosphatase F I
Products: -
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CMP + H2O
cytidine + phosphate
-
Substrates: alkaline phosphatase F II
Products: -
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?
cytidine 5'-monophosphate + H2O
?
Substrates: 343.8% of the activity with 4-nitrophenyl phosphate
Products: -
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cytidine 5'-monophosphate + H2O
?
Substrates: 343.8% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
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D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
Substrates: 36% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
Substrates: 5.2% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
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D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
Substrates: wild-type activity is 2.2% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 52fold higher than activity from wild-type enzyme
Products: -
Products: -
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D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
Substrates: -
Products: -
Products: -
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
Substrates: 32% of the activity with 4-nitrophenyl phosphate
Products: -
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?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
Products: -
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
Bacillus licheniformis MTCC 1483
Substrates: -
Products: -
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D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
Substrates: wild-type activity is 9.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 21fold higher than activity from wild-type enzyme
Products: -
Products: -
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D-glucose 1-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
Products: -
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
A0A196MRA0
Substrates: 36.0% of the activity with 4-nitrophenyl phosphate
Products: -
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D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
Substrates: 60% of the activity with 4-nitrophenyl phosphate
Products: -
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D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
Substrates: 19.4% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
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D-glucose 6-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Bacillus licheniformis MTCC 1483
Substrates: -
Products: -
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D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
Substrates: wild-type activity is 6.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 34.5fold higher than activity from wild-type enzyme
Products: -
Products: -
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D-glucose 6-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
A0A196MRA0
Substrates: 34.1% of the activity with 4-nitrophenyl phosphate
Products: -
Products: -
?
D-glucose-6-phosphate + H2O
D-glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
D-glucose-6-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
Products: -
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
Substrates: -
Products: -
Products: -
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
Substrates: -
Products: -
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?
diphosphate + H2O
2 phosphate
-
Substrates: alkaline phosphatase F I
Products: -
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?
diphosphate + H2O
2 phosphate
-
Substrates: alkaline phosphatase F II
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diphosphate + H2O
2 phosphate
A0A196MRA0
Substrates: 46.7% of the activity with 4-nitrophenyl phosphate
Products: -
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glucose 1-phosphate + H2O
glucose + phosphate
-
Substrates: 93% of the activity with 4-nitrophenyl phosphate
Products: -
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?
glucose 1-phosphate + H2O
glucose + phosphate
-
Substrates: -
Products: -
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?
glucose 1-phosphate + H2O
glucose + phosphate
-
Substrates: -
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Products: -
?
glucose 1-phosphate + H2O
glucose + phosphate
-
Substrates: -
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Products: -
?
glucose 1-phosphate + H2O
glucose + phosphate
-
Substrates: -
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?
glucose 1-phosphate + H2O
glucose + phosphate
-
Substrates: -
Products: -
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?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
Substrates: alkaline phosphatase F I
Products: -
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?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
Substrates: alkaline phosphatase F II
Products: -
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?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
Substrates: -
Products: -
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?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
Substrates: -
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glycerophosphate + H2O
glycerol + phosphate
-
Substrates: 63% of the activity with 4-nitrophenyl phosphate
Products: -
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glycerophosphate + H2O
glycerol + phosphate
-
Substrates: -
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GMP + H2O
guanosine + phosphate
-
Substrates: alkaline phosphatase F I
Products: -
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GMP + H2O
guanosine + phosphate
-
Substrates: alkaline phosphatase F II
Products: -
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guanosine 5'-monophosphate + H2O
?
Substrates: 358.8% of the activity with 4-nitrophenyl phosphate
Products: -
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guanosine 5'-monophosphate + H2O
?
Substrates: 358.8% of the activity with 4-nitrophenyl phosphate
Products: -
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L-histidinyl phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
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?
L-histidinyl phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
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linear DNA fragment + H2O
dephosphorylated linear DNA fragment + phosphate
Substrates: the enzyme has a dephosphorylation efficiency of 92.9% to dephosphorylate linear DNA fragments of plasmid pUC18
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linear DNA fragment + H2O
dephosphorylated linear DNA fragment + phosphate
Bacillus licheniformis MTCC 1483
Substrates: the enzyme has a dephosphorylation efficiency of 92.9% to dephosphorylate linear DNA fragments of plasmid pUC18
Products: -
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methyl phosphate + H2O
methanol + phosphate
Substrates: -
Products: -
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O-phosphoserine + H2O
serine + phosphate
-
Substrates: -
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O-phosphoserine + H2O
serine + phosphate
Substrates: -
Products: -
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O-phosphoserine + H2O
serine + phosphate
-
Substrates: wild-type activity is 14.0% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 10.9fold higher than activity from wild-type enzyme
Products: -
Products: -
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O-phosphothreonine + H2O
threonine + phosphate
-
Substrates: -
Products: -
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O-phosphothreonine + H2O
threonine + phosphate
-
Substrates: wild-type activity is 21.3% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 9.8fold higher than activity from wild-type enzyme
Products: -
Products: -
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O-phosphotyrosine + H2O
tyrosine + phosphate
-
Substrates: -
Products: -
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O-phosphotyrosine + H2O
tyrosine + phosphate
Substrates: -
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O-phosphotyrosine + H2O
tyrosine + phosphate
-
Substrates: wild-type activity is 68.3% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 8.6fold higher than activity from wild-type enzyme
Products: -
Products: -
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
antarctic bacterium
-
Substrates: -
Products: -
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
antarctic bacterium HK47
-
Substrates: -
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: hydrolyzed by isoenzyme I, II or III
Products: -
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
Substrates: activities towards tyrosine phosphatase substrate ENCpYINASL and calcineurin substrate DLDVPIPGRDFRRVpSVAAE were also detected, further substrates: ATP, sn-glycerol 3-phosphate
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
Synechococcus elongatus PCC 7942 = FACHB-805 R2
-
Substrates: -
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Products: -
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
-
Substrates: -
Products: -
Products: -
?
phenyl phosphate + H2O
phenol + phosphate
-
Substrates: -
Products: -
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?
phenyl phosphate + H2O
phenol + phosphate
-
Substrates: -
Products: -
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?
phenyl phosphate + H2O
phenol + phosphate
Substrates: -
Products: -
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?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
Substrates: -
Products: -
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?
phosphoenolpyruvate + H2O
pyruvate + phosphate
Substrates: -
Products: -
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?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
Substrates: -
Products: -
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?
phosphoethanolamine + H2O
phosphate + ethanolamine
-
Substrates: hydrolyzed by isoenzyme III, weak activity with isoenzyme II, no activity with isoenzyme I
Products: -
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?
phosphoethanolamine + H2O
phosphate + ethanolamine
-
Substrates: -
Products: -
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?
phosphoethanolamine + H2O
phosphate + ethanolamine
-
Substrates: -
Products: -
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?
phosphoethanolamine + H2O
phosphate + ethanolamine
-
Substrates: -
Products: -
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?
phosphorylated acetyl-CoA carboxylase + H2O
acetyl-CoA carboxylase + phosphate
-
Substrates: -
Products: -
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?
phosphorylated acetyl-CoA carboxylase + H2O
acetyl-CoA carboxylase + phosphate
-
Substrates: -
Products: -
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phosphorylcholine + H2O
phosphate + choline
-
Substrates: hydrolyzed by isoenzyme III, no activity with isoenzyme I and II
Products: -
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phosphorylcholine + H2O
phosphate + choline
-
Substrates: -
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?
phosphoserine + H2O
phosphate + Ser
-
Substrates: 9.3% of the activity with 4-nitrophenyl phosphate
Products: -
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?
phosphoserine + H2O
phosphate + Ser
-
Substrates: hydrolyzed by isoenzyme II, weak activity with isoenzyme I and II
Products: -
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?
phosphoserine + H2O
phosphate + Ser
-
Substrates: -
Products: -
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?
UMP + H2O
uridine + phosphate
-
Substrates: alkaline phosphatase F I
Products: -
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?
UMP + H2O
uridine + phosphate
-
Substrates: alkaline phosphatase F II
Products: -
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?
UTP + H2O
?
-
Substrates: 67% of the activity with 4-nitrophenyl phosphate
Products: -
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?
additional information
?
-
-
Substrates: the purified alkaline phosphatase removes the 5'-phosphate group of a linearized plasmid without showing DNAase activity
Products: -
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?
additional information
?
-
-
Substrates: motion required for the formation of the enzyme-phosphate complex is minimal on the part of alkaline phosphatase
Products: -
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?
additional information
?
-
-
Substrates: TNAP is an essential component of serum calcification activity and that its role in the shotgun mechanism is to activate the serum nucleator of apatite crystal formation
Products: -
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?
additional information
?
-
-
Substrates: enzmye exclusively phosphomonoesters as a substrate, and not phosphodiesters
Products: -
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?
additional information
?
-
-
Substrates: alkaline phosphatase activity is decreased during vitamin C deficiency. The decreased expression of collagen, alkaline phosphatase, and osteocalcin can explain the defects in bone caused by scurvy
Products: -
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?
additional information
?
-
-
Substrates: could be a component of muscle regulatory mechanism at the biochemical level secondary to hyper-regulation of Chasmagnathus granulatus
Products: -
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?
additional information
?
-
-
Substrates: the enzyme is involved in the biochemical amplification process of excitation or adaption
Products: -
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?
additional information
?
-
-
Substrates: involvement of the enzyme in sugar metabolism
Products: -
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?
additional information
?
-
-
Substrates: the enzyme also catalyses the transfer of the phosphoryl group to alcohols
Products: -
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?
additional information
?
-
-
Substrates: the enzyme is involved in recovering of phosphate esters when free phosphate is depleted
Products: -
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?
additional information
?
-
-
Substrates: the enzyme catalyzes the oxidation of phosphite to phosphate and molecular H2: H2PO3 + H2O = H3PO4 + H2
Products: -
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?
additional information
?
-
-
Substrates: HcALP is a Cry1Ac binding protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is impportant in bone formation and mineralization
Products: -
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?
additional information
?
-
-
Substrates: the enzyme is necessary for the initiation of mineralization by osteoblast-derived matrix vesicles but not for the continuation of the processes
Products: -
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?
additional information
?
-
-
Substrates: hypophosphatasia is an inherited disorder caused by mutations in the bone alkaline phosphatase gene
Products: -
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?
additional information
?
-
-
Substrates: hypophosphatasia is caused by deficiency of activity of the tissue-nonspecific alkaline phosphatase, resulting in a defect of bone mineralization
Products: -
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?
additional information
?
-
-
Substrates: involvement of androgen receptor positive chondrocytes in thyroid cartilage mineralization, probably by a testosterone-linked stimulation of alkaline phosphatase
Products: -
Products: -
?
additional information
?
-
-
Substrates: strong correlations between ALP activity and lipid accumulation. These data suggest that ALP and fat storage are tightly linked during preadipocyte maturation
Products: -
Products: -
?
additional information
?
-
-
Substrates: IAP possesses lipopolysaccharide-dephosphorylating activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is important in bone formation and mineralization
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the regulation of mineralization of cartilage matrix
Products: -
Products: -
?
additional information
?
-
-
Substrates: strong correlations between ALP activity and lipid accumulation. These data suggest that ALP and fat storage are tightly linked during preadipocyte maturation
Products: -
Products: -
?
additional information
?
-
-
Substrates: levamisole-insensitive alkaline phosphatase activity could be a component of muscle regulatory mechanism at the biochemical level secondary to hyper-regulation of Chasmagnathus granulatus
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of diphosphate
Products: -
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?
additional information
?
-
-
Substrates: enzyme with limited substrate specificity, no dephosphorylation of ATP, PEP, glucose 6-phosphate, phosphoinositol 4',5'-bisphosphate, phosphoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a nonspecific phosphomonoesterase that functions through a phosphoseryl intermediate to produce free inorganic phosphate or to transfer the phosphoryl group to other alcohols
Products: -
Products: -
?
additional information
?
-
-
Substrates: a low level of high-molecular weight alkaline phosphatase is produced constitutively, low-molecular weight alkaline phosphatase is produced only after induction
Products: -
Products: -
?
additional information
?
-
-
Substrates: important enzyme in the final stages of cell division when Pseudomonas aeruginosa is cultured in inorganic phosphate-limiting media
Products: -
Products: -
?
additional information
?
-
-
Substrates: high-molecular weight alkaline phosphatase is active as phosphomonoesterase, low-molecular weight alkaline phosphatase is active as phosphomonoesterase and phosphodiesterase
Products: -
Products: -
?
additional information
?
-
-
Substrates: a low level of high-molecular weight alkaline phosphatase is produced constitutively, low-molecular weight alkaline phosphatase is produced only after induction
Products: -
Products: -
?
additional information
?
-
-
Substrates: high-molecular weight alkaline phosphatase is active as phosphomonoesterase, low-molecular weight alkaline phosphatase is active as phosphomonoesterase and phosphodiesterase
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also dephosphorylizes cohesive and blunt ends of DNA fragments, cohesive ends are slightly preferred
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?
additional information
?
-
-
Substrates: the enzyme also dephosphorylizes cohesive and blunt ends of DNA fragments, cohesive ends are slightly preferred
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?
additional information
?
-
-
Substrates: enzyme is impportant in bone formation and mineralization
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?
additional information
?
-
-
Substrates: non-specific enzyme, wide substrate specificity, no phosphate transfer with alcohols, except for Tris
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?
additional information
?
-
-
Substrates: the product of the PHO8 gene is repressible by phosphate in the medium
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?
additional information
?
-
-
Substrates: non-specific enzyme, wide substrate specificity, no phosphate transfer with alcohols, except for Tris
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?
additional information
?
-
A0A196MRA0
Substrates: very poor substrate: bis(4-nitrophenyl) phosphate
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-
additional information
?
-
Substrates: with acceptors 1,4-butanediol, mono- and oligosaccharides, nucleosides, rac-serine and rac-mevalonic acid at pH9, very low phosphate transfer efficiencies (max. 5%) are observed
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-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
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?
additional information
?
-
-
Substrates: TNAP is an essential component of serum calcification activity and that its role in the shotgun mechanism is to activate the serum nucleator of apatite crystal formation
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?
additional information
?
-
-
Substrates: alkaline phosphatase activity is decreased during vitamin C deficiency. The decreased expression of collagen, alkaline phosphatase, and osteocalcin can explain the defects in bone caused by scurvy
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?
additional information
?
-
-
Substrates: could be a component of muscle regulatory mechanism at the biochemical level secondary to hyper-regulation of Chasmagnathus granulatus
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?
additional information
?
-
-
Substrates: the enzyme is involved in the biochemical amplification process of excitation or adaption
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?
additional information
?
-
-
Substrates: involvement of the enzyme in sugar metabolism
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?
additional information
?
-
-
Substrates: the enzyme is involved in recovering of phosphate esters when free phosphate is depleted
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?
additional information
?
-
-
Substrates: HcALP is a Cry1Ac binding protein
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?
additional information
?
-
-
Substrates: enzyme is impportant in bone formation and mineralization
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?
additional information
?
-
-
Substrates: the enzyme is necessary for the initiation of mineralization by osteoblast-derived matrix vesicles but not for the continuation of the processes
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?
additional information
?
-
-
Substrates: hypophosphatasia is an inherited disorder caused by mutations in the bone alkaline phosphatase gene
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?
additional information
?
-
-
Substrates: hypophosphatasia is caused by deficiency of activity of the tissue-nonspecific alkaline phosphatase, resulting in a defect of bone mineralization
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?
additional information
?
-
-
Substrates: involvement of androgen receptor positive chondrocytes in thyroid cartilage mineralization, probably by a testosterone-linked stimulation of alkaline phosphatase
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?
additional information
?
-
-
Substrates: strong correlations between ALP activity and lipid accumulation. These data suggest that ALP and fat storage are tightly linked during preadipocyte maturation
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?
additional information
?
-
-
Substrates: enzyme is important in bone formation and mineralization
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?
additional information
?
-
-
Substrates: the enzyme is involved in the regulation of mineralization of cartilage matrix
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?
additional information
?
-
-
Substrates: strong correlations between ALP activity and lipid accumulation. These data suggest that ALP and fat storage are tightly linked during preadipocyte maturation
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?
additional information
?
-
-
Substrates: levamisole-insensitive alkaline phosphatase activity could be a component of muscle regulatory mechanism at the biochemical level secondary to hyper-regulation of Chasmagnathus granulatus
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?
additional information
?
-
-
Substrates: a low level of high-molecular weight alkaline phosphatase is produced constitutively, low-molecular weight alkaline phosphatase is produced only after induction
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?
additional information
?
-
-
Substrates: important enzyme in the final stages of cell division when Pseudomonas aeruginosa is cultured in inorganic phosphate-limiting media
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?
additional information
?
-
-
Substrates: a low level of high-molecular weight alkaline phosphatase is produced constitutively, low-molecular weight alkaline phosphatase is produced only after induction
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?
additional information
?
-
-
Substrates: enzyme is impportant in bone formation and mineralization
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?
additional information
?
-
-
Substrates: the product of the PHO8 gene is repressible by phosphate in the medium
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
Ba2+
Ca2+
Co2+
Cu2+
Fe2+
Fe3+
K+
KCl
Mg2+
Mn2+
Na+
NaCl
Ni2+
sulfate
-
the rate of irreversible thermal inactivation is strongly reduced by addition of kosmotropic anions like sulfate (half-life increases from 8 to 580 min at 60 °C)
Zn
Zn2+
additional information
Al3+
-
inhibits high molecular weight and low molecular weight alkaline phosphatase non-competitively
Ca2+
-
requires Ca2+ and not Zn2+ ions for its activity.Optimal Ca2+ concentration for enzymatic activity is 3.4 mM
Ca2+
activates. D527 of PhoX might be the ligand bound to the catalytic calcium
Ca2+
-
partly restores enzymatic activity after EDTA treatment. When Mg2+ is combined with Zn2+, it enhances the catalytic activity up to 3fold
Ca2+
A0A196MRA0
protein contains approximately two Ca2+ and one Zn2+ per monomer. In presence of 1 mM Ca2+, 83.8% of initial activity
Co2+
required. In the absence of Co2+ in the lysis buffer, activity of extracts is only 10% of the normal value
Co2+
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
Co2+
-
26% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0022 mM for wild-type enzyme, 0.00051 mM for mutant os-1 enzyme
Co2+
-
50fold increase in activity compared with activity before EDTA treatment
Co2+
-
metalloenzyme, dependent on, can partially be substituted by Mg2+ and Mn2+
Co2+
-
enhances activity, twice as active than with either Zn2+ or Mn2+
Co2+
-
activity is dependent on metal ion, Co2+ is the most active stimulator and has unique effect at high temperature
K+
-
the kinetic behaviour is determined by the ratio between concentration of Mn2+ and concentration of Na+ or K+. When the Mn2+ increases and Na+ or K+ decreases, the kinetics show cooperative behaviour
Mg2+
-
metalloenzyme containing Mg2+ and Zn2+ with a molar ratio of 1:2, enzyme exhibits 1.6fold activation in the presenece of 1 mM Co2+
Mg2+
-
isoenzyme C1, C2, and B2 contain 6 gatoms of Zn per dimer, removal results in loss of activity
Mg2+
-
stimulates, required for maintenance of activity at high concentrations of Na+
Mg2+
-
enzyme contains 1 Mg2+ ion per monomer, located near the active site, interacting with phosphate
Mg2+
removal of a third metal ion site near the bimetallo site, containing Mg2+, suggests that the Mg2+ ion participates in general base catalysis. Mg2+ ion stabilizes the transferred phosphoryl group in the transition state, and this interaction is distinct from those mediated by the Zn2+ bimetallo site. Positioning of charged or polar groups to interact with all three nonbridging oxygen atoms of the transferred phosphoryl group is important for catalysis of phosphate monoester hydrolysis
Mg2+
-
bivalent metal ions required, maximal enhancement in presence of Mg2+
Mg2+
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
Mg2+
metal-binding site M3, consisting of residues Asp12, Thr118 and Glu264. Metal-binding site M5 site is composed of at least five chelating O atoms, from the main chain of Gly103, O1 of Asp255 and O2 of Asp257 and two O atoms from water molecules, weakly chelating Mg2+
Mg2+
-
80% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0036 mM for wild-type enzyme, 0.0084 mM for mutant os-1 enzyme
Mg2+
-
non-essential mixed-type activator, half-maximal effect at 0.007 mM
Mg2+
-
partly restores enzymatic activity after EDTA treatment. When Mg2+ is combined with Zn2+, it enhances the catalytic activity up to 3fold
Mg2+
-
metalloprotein contains Zn2+ and Mg2+, both of which are necessary for catalytic function
Mg2+
-
2fold activation at 10 mM, dependent on, if 4-nitrophenyl phosphate is used as a substrate, protein phosphatase activity is not Mg2+-dependent
Mg2+
-
activity is greatly enhanced by simultaneous addition of Mg2+ and Zn2+. Maximal specific activity in presence of 20 mM MgCl2 and 5 mM ZnCl2
Mg2+
0.1 mM, 1.3fold increase in activity. 2 mM, 1.6fold increase in activity
Mg2+
-
activity is dependent on metal ion, Co2+, Mg2+ and Zn2+ are the main activators
Mg2+
-
wild-type enzyme most likely has one Mg2+ in the active site in addition to three Mg2+ that bind elsewhere. At 18°C with 10 mM Mg2+, the enzyme activity is completely stable over 160 min. With no Mg2+ in solution, the activity drops to 20% of the initial activity after 160 min
Mn2+
-
the kinetic behaviour is determined by the ratio between concentration of Mn2+ and concentration of Na+ or K+. When the Mn2+ increases and Na+ or K+ decreases, the kinetics show cooperative behaviour
Na+
-
the kinetic behaviour is determined by the ratio between concentration of Mn2+ and concentration of Na+ or K+. When the Mn2+ increases and Na+ or K+ decreases, the kinetics show cooperative behaviour
Na+
-
gel filtration fraction is converted to the native structure by Na2SO4 suggesting the importance of Na ion
NaCl
presence of 0.5 M NaCl increases the melting temperature of wild-type protein by about 20%
Ni2+
-
23% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0019 mM for wild-type enzyme, 0.0037 mM for mutant os-1 enzyme
Zn2+
-
enzyme contains 2 Zn2+ ions per monomer, located near the active site, interacting with phosphate
Zn2+
-
the enzyme employs a binuclear metallocenter of two Zn2+ ions approximately 4 A apart to facilitate catalysis of phosphate monoester hydrolysis. Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions
Zn2+
-
strong support for a model in which electrostatic interactions between the bimetallo Zn2+ site and a nonbridging phosphate ester oxygen atom make a significant contribution to the large rate enhancement observed for alkaline phosphatase-catalyzed phosphate monoester hydrolysis
Zn2+
metalloenzyme, mutant T59A contains sn amount similar to the wild-type enzyme, while mutant T59R has almost undetectable amounts of bound metal
Zn2+
removal of a third metal ion site near the bimetallo site, containing Mg2+, suggests that the Mg2+ ion participates in general base catalysis. Mg2+ ion stabilizes the transferred phosphoryl group in the transition state, and this interaction is distinct from those mediated by the Zn2+ bimetallo site. Positioning of charged or polar groups to interact with all three nonbridging oxygen atoms of the transferred phosphoryl group is important for catalysis of phosphate monoester hydrolysis
Zn2+
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
Zn2+
metal-binding site M1 site consists of residues Asp269, His273 and His461, in which Zn2+ is chelated by three O and two N atoms with distances of 2.12.5 A. In the metal-binding site M2 residues Asp12, Ser65, Asp311 and His312 Zn2+ is chelated by five O atoms and one N atom with distances of 2.0-2.1 A
Zn2+
-
metalloprotein contains Zn2+ and Mg2+, both of which are necessary for catalytic function
Zn2+
-
activity is greatly enhanced by simultaneous addition of Mg2+ and Zn2+. Maximal specific activity in presence of 20 mM MgCl2 and 5 mM ZnCl2
Zn2+
A0A196MRA0
protein contains approximately two Ca2+ and one Zn2+ per monomer. In presence of 1 mM Zn2+, 6% of initial activity
Zn2+
-
activity is dependent on metal ion, Co2+, Mg2+ and Zn2+ are the main activators
Zn2+
-
wild-type enzyme most likely has two Zn2+. Zn2+ release from the active site coincides with total protein structure unfolding
additional information
enzyme does not require the presence of exogenous divalent cations
additional information
-
enzyme does not require the presence of exogenous divalent cations
additional information
-
each subunit contains an active centre with three distinct metal binding sites and one phosphorylatable Ser
additional information
metal-binding site M4 site is composed of six O atoms from the main chains of Ala45, Lys46, Gly48 and Ser481, the O atom of Ser482 and one water O atom, chelating a metal ion with distances of 2.2-2.7 A
additional information
-
enzyme does not require presence of zinc ions
additional information
-
the SWISS-MODEL program is used to construct a model of isoenzyme rIAP-I. Analysis of the active site of the enzyme and the effect of various combinations of metals at the active site. The model shows the possibility of a Zn triad at the metal-binding position of the active site in rIAP-I
additional information
-
the SWISS-MODEL program is used to construct a model of isoenzyme rIAP-II. Analysis of the active site of the enzyme and the effect of various combinations of metals at the active site
additional information
-
not affected by F- at 10 mM, protein phosphatase activity is not Mg2+-dependent
additional information
presence of divalent cation is required. Enzyme activity is strongly affected by rising metal ion concentration in carbonate, Tris and CHES (N-cyclohexyl-2-aminoethanesulfonic acid) buffers but not in glycine buffer, in which the activity could be significantly improved with up to 5mM salt
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-(2,4-dimethylphenyl)prop-2-en-1-one
-
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-(3-methoxy-4-propoxyphenyl)prop-2-en-1-one
-
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-(4-fluorophenyl)prop-2-en-1-one
-
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-(4-methoxyphenyl)prop-2-en-1-one
-
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-(thiophen-2-yl)prop-2-en-1-one
-
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-[4-(dimethylamino)phenyl]prop-2-en-1-one
-
(2E)-2-[4-(benzyloxy)-[3-methoxyphenyl]methylidene]-6-chloro-4-nitro-1-benzofuran-3(2H)-one
-
-
(2E)-3-[4-(benzyloxy)-3-methoxyphenyl]-1-(5-chloro-2-hydroxy-3-nitrophenyl)prop-2-en-1-one
-
(2E)-4,6-dibromo-2-[[4-(trifluoromethyl)phenyl]methylidene]-1-benzofuran-3(2H)-one
-
(2E)-6-chloro-2-[(2,4-dimethylphenyl)methylidene]-4-nitro-1-benzofuran-3(2H)-one
-
(2E)-6-chloro-2-[(3-methoxy-4-propoxyphenyl)methylidene]-4-nitro-1-benzofuran-3(2H)-one
-
(2E)-6-chloro-2-[(4-chlorophenyl)methylidene]-4-nitro-1-benzofuran-3(2H)-one
-
(2E)-6-chloro-2-[[4-(dimethylamino)phenyl]methylidene]-4-nitro-1-benzofuran-3(2H)-one
-
(2E)-6-chloro-4-nitro-2-[(thiophen-2-yl)methylidene]-1-benzofuran-3(2H)-one
-
(2Z)-2-(benzoylamino)-3-[2-[4-(trifluoromethyl)phenyl]-1-benzothiophen-3-yl]prop-2-enoate
-
with 0.1 mM 35% remaining activity
(4-methoxyphenyl)[2-(4-methoxyphenyl)-1-benzothiophen-3-yl]methanone
-
with 0.1 mM 70% remaining activity
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
-
(E)-N'-(4'-chlorobenzylidene)isonicotinohydrazide
most potent inhibitor for intestinal alkaline phosphatase
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
most potent inhibitor for tissue-non-specific alkaline phosphatase
1-(2,4-dihydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
selective for intestinal isoform
1-(3,4-dihydroxyphenyl)-2-[(4-methyl-5-phenyl-4H-1,2,4-triazol-3-yl)sulfanyl]ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
-
-
1-(3,4-dimethoxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
selective for intestinal isoform
1-(3-hydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
inhibits both intestinal and tissue-nonspecific isoform; inhibits both intestinal and tissue-nonspecific isoform
1-(4-chlorobenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
inhibits both intestinal and tissue-nonspecific isoform; inhibits both intestinal and tissue-nonspecific isoform
1-(4-hydroxy, 3-methoxybenzylidene)-2-(4-tertbutylthiazol-2-yl)hydrazine
inhibits both intestinal and tissue-nonspecific isoform; inhibits both intestinal and tissue-nonspecific isoform
1-(4-hydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
inhibits both intestinal and tissue-nonspecific isoform; inhibits both intestinal and tissue-nonspecific isoform
1-(4-tert-butylthiazol-2-yl)-2-(furan-2-ylmethylene)hydrazine
selective for intestinal isoform
1-(5-bromo,2-hydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
-
1-benzothiophen-3-yl(4-methoxyphenyl)methanone
-
with 0.1 mM 40% remaining activity
2,4,6-Trinitrobenzenesulfonic acid
-
enzyme loses 80% of its initial activity after incubation for 30 min with 1.0 mM 2,4,6-trinitrobenzenesulfonic acid in bicarbonate buffer, pH 9.0 at 25°C. Increasing concentration can not result in more loss of activity
2,4-dichloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
2,6-diamino-1-benzyl-4-(2,3,4-trimethoxyphenyl)-1,4-dihydropyridine-3,5-dicarbonitrile
IC50 value for growth inhibition of HeLa cell is 0.0695 mM
2,6-diamino-1-benzyl-4-(3-hydroxy-2-methoxyphenyl)-1,4-dihydropyridine-3,5-dicarbonitrile
IC50 value for growth inhibition of HeLa cell is 0.0570 mM, for MCF-7 cell 0.0770 mM, respectively
2,6-diamino-1-benzyl-4-(naphthalen-2-yl)-1,4-dihydropyridine-3,5-dicarbonitrile
compound plays a significant role in inducing apoptosis through multiple mechanisms. IC50 value for growth inhibition of HeLa cell is 0.0535 mM, for MCF-7 cell 0.0387 mM, respectively
2-((3-(1H-imidazol-1-yl)propyl)amino)-6-amino-4-(4-ethoxyphenyl)pyridine-3,5-dicarbonitrile
IC50 value for growth inhibition of HeLa cell is 0.0570 mM, for MCF-7 cell 0.0540 mM, respectively
2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)-N-(3-(trifluoromethyl)phenyl)acetamide
noncompetitive. Compound exhibits excellent binding affinity and is nontoxic
2-(1-methylhydrazenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(2-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 63% remaining activity
2-(2-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(2-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(2-methoxyphenyl)-7- trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(2-methylphenyl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 5% remaining activity
2-(2-nitrophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.4 mM 78% remaining activity
2-(3,4-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3,5-di-methoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3,5-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 62% remaining activity
2-(3-cyanophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-fluoromethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-formyl-1-benzothiophen-2-yl)benzonitrile
-
with 0.4 mM 79% remaining activity
2-(3-methoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-nitrophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-phenylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-aminophenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 9% remaining activity
2-(4-chlorophenyl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 69% remaining activity
2-(4-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-ethoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-ethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-i-propylphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-methoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-methoxyphenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 37% remaining activity
2-(4-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-trifluoromethoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]piperazin-1-yl)ethanol
-
2-(naphthalen-2-yl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 18% remaining activity
2-(pyridin-3-yl)-1-benzothiophene-3-carbaldehyde
-
with 0.4 mM 79% remaining activity
2-([(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)sulfonyl]amino)-N-(2,5-dimethylphenyl)acetamide
potent inhibitor with good selectivity against both placental and tissue-nonspecific alkaline phosphatase, competitive inhibition. A dose of 10 microM completley inhibits the enzyme expressed by transfected COS-1 cells
2-allylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-di-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-isopropyl-5-methylphenyl 2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)acetate
-
2-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-n-pentylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-n-propylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-phenyl-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-[2-(dimethylamino)ethyl]amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-[3-(2,2,2-trifluoroethyl)-1-benzothiophen-2-yl]benzonitrile
-
with 0.1 mM 70% remaining activity
2-[3-(4-chlorophenoxy)-1-benzothiophen-2-yl]benzonitrile
-
with 0.4 mM 79% remaining activity
2-[3-(4-fluorophenoxy)-1-benzothiophen-2-yl]benzonitrile
-
with 0.1 mM 66% remaining activity
2-[4-(1-benzothiophen-3-yl)piperazin-1-yl]phenol
-
with 0.1 mM 49% remaining activity
2-[4-(trifluoromethyl)phenyl]-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 30% remaining activity
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
-
-
3-(2,4-dichloro-5-fluorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
-
3-methoxy-2-(2-methylphenyl)-1-benzothiophene
-
with 0.1 mM 73% remaining activity
3-methoxy-2-(4-methoxyphenyl)-1-benzothiophene
-
with 0.1 mM 78% remaining activity
4-(2-((6-amino-3,5-dicyano-4-(4-ethoxyphenyl)pyridine-2yl)amino)ethyl)benzene sulfonamide
IC50 value for growth inhibition of HeLa cell is 0.0630 mM, for MCF-7 cell 0.0980 mM, respectively
4-[(1-oxido-1-benzothiophen-3-yl)oxy]benzonitrile
-
with 0.4 mM 67% remaining activity
4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)-methyl]-N-(2-methylphenyl)benzamide
-
4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)-methyl]-N-(3-methylphenyl)benzamide
-
4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)-methyl]-N-(4-methylphenyl)benzamide
-
5-((5-chloro-2-methoxyphenyl)sulfonamido)nicotinamide
SBI-425, potent inhibitor
5-chloro-2-methoxy-N-[5-(2-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
-
5-chloro-2-methoxy-N-[5-(3-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
-
5-chloro-2-methoxy-N-[5-(4-methoxyphenyl)pyridin-3-yl]benzene-1-sulfonamide
-
5-chloro-2-methoxy-N-[5-(4-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
-
5-chloro-2-methoxy-N-[5-(4-methylpiperazine-1-carbonyl)pyridin-3-yl]benzene-1-sulfonamide
-
5-chloro-N-[5-(4-chlorophenyl)pyridin-3-yl]-2-methoxybenzene-1-sulfonamide
-
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-ethylpyridine-3-carboxamide
-
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-methylpyridine-3-carboxamide
-
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-phenylpyridine-3-carboxamide
-
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxamide
SBI-425, potent inhibitor
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxylic acid
-
5-[[2-methoxy-5-(trifluoromethoxy)benzene-1-sulfonyl]amino]pyridine-3-carboxamide
-
5-[[5-chloro-2-(trifluoromethoxy)benzene-1-sulfonyl]amino]pyridine-3-carboxamide
-
6-(1-benzothiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
-
with 0.4 mM 19% remaining activity
6-(1-benzothiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole
-
with 0.4 mM 11% remaining activity
6-(5-nitro-1-benzothiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
-
alendronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
artemether
-
6 mg/l artemether has significant inhibitory effects on extracellular enzyme activity
CO2
-
enzyme in buffer can be inactivated by COS treatment at atmospheric pressure, increasing inactivation, when temperature increases from 20°C to 50°C, 16% loss of activity after 30 min at 20°C, 81% loss of activity after 30 min at 50°C. Change in activity dependent on CO2 treatment is not observed in raw milk mainly due to strong buffering capacity of milk
Cry1Ac toxin
environment friendly insecticidal crystal proteins encoded by the spore-forming bacteria Bacillus thuringiensis. Competitive inhibitor; environment friendly insecticidal crystal proteins encoded by the spore-forming bacteria Bacillus thuringiensis. Competitive inhibitor
-
Cyclohexylamine
noncompetitive. At pH 9.8, inhibition is not sensitive to 0.5 M NaCl. At pH 8.0, the addition of 0.5 M NaCl alters the inhibition to the level observed at pH 9.8
dihydroartemisinin
-
24 mg/l dihydroartemisinin has significant inhibitory effects on extracellular enzyme activity
guanidine hydrochloride
-
inactivation of the enzyme by GuHCl (guanidine hydrochloride) is a slow, reversible reaction with fractional remaining activity. The microscopic rate constants are determined. The enzyme is protected by the substrate to a certain extent during guanidine denaturation. The changes of conformation of the enzyme in different concentrations of GuHCl are studied. The inactivation occurs before the noticeable conformational changes of the enzyme molecule as a whole can be detected, which suggests that the active site of the enzyme has more flexibility than the whole enzyme molecule
Imipenem
inhibition is time dependent reaching about 98% in 30 min on ice at 1.2 mM and 95% at 0.24 mM
L-amino acids
specific uncompetitive inhibition, molecular mechanism involves Arg166 and Glu429
lectin
5 g/L, precipitation by lectin: 100%; 5 g/L, precipitation by lectin: 100%; 5 g/L, precipitation by lectin: 100%, bone isoenzyme; 5 g/L, precipitation by lectin: 58%, isoenzyme rTI2B; 5 g/L, precipitation by lectin: 76%, isoenzyme rTI2A
-
methyl (2E)-2-(benzoylamino)-3-[2-(4-methoxyphenyl)-1-benzothiophen-3-yl]prop-2-enoate
-
with 0.1 mM 77% remaining activity
methyl 3-(1-benzothiophen-3-yl)-N-benzoylalaninate
-
with 0.4 mM 74% remaining activity
methyl 5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxylate
-
methyl N-benzoyl-3-[2-[4-(trifluoromethyl)phenyl]-1-benzothiophen-3-yl]alaninate
-
with 0.1 mM 63% remaining activity
N-(2,3-dimethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
-
N-(2,4-dimethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
-
N-(2,6-dimethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
-
N-(2-ethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
-
N-(3,4-dimethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
-
N-(3,5-dimethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
-
N-(3-cyanophenyl)-3-([(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)sulfonyl]amino)propanamide
potent inhibitor with good selectivity against both placental and tissue-nonspecific alkaline phosphatase
N-(3-ethoxyphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
-
N-(4-ethoxyphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
noncompetitive
NaWO4
-
1 mM NaWO4, 35% inhibition of isoenzyme I, 80% inhibition of isoenzyme II, 14% inhibition of isoenzyme III
pamidronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
PCMB
-
1 mM, 54% inhibition of isoenzyme I, 33% inhibition of isoenzyme II, 9% inhibition of isoenzyme III
Phenylglyoxal
-
1.0 mM, complete irreversible inactivation after 30 min in bicarbonate buffer, pH 9.0, at 25°C
phenylphosphonate
-
10 mM, 47% inhibition of p-nitrophenyl phosphate hydrolysis, 80% inhibition of dephosphorylation of P-labelled histones
Sodium acetate
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
Sodium citrate
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
zoledronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
2-(3-methoxy-1-benzothiophen-2-yl)benzonitrile
-
with 0.1 mM 57% remaining activity
2-(3-methoxy-1-benzothiophen-2-yl)benzonitrile
-
with 0.4 mM 79% remaining activity
2-mercaptoethanol
-
the P2 isoenzyme is more sensitive to 2-mercaptoethanol than P1
arsenate
-
1 mM Na2HAsO4, 80% inhibition of isoenzyme I, 22% inhibition of isoenzyme II, 40% inhibition of isoenzyme III
Borate
-
1 mM H3BO4, 16% inhibition of isoenzyme I, 13% inhibition of isoenzyme II, 8% inhibition of isoenzyme III
Ca2+
-
in presence of 0.005 mM Mg2+, Ca2+ acts as an uncompetitive inhibitor, at 0.1 mM Mg2+, Ca2+ inhibits non-competitively
Cd2+
-
chronic cadmium exposure (32.5 ppm Cd2+ in purified water over 3 months) leads to noncompetitive inhibition of serum and hepatic enzyme activity. The addition of 5 mM of Zn2+ shows almost 58% reactivation of the enzyme
Cd2+
-
39% inhibition of the enzyme at 1 mM in the gills, but not in digestive gland
corticosterone
-
5 mM, 90% inhibition of alkaline phosphatase grown in high phosphate medium, no effect is observed with alkaline phosphatase grown in low phosphate medium
Cu2+
-
1 mM, 87% inhibition of isoenzyme I, 10% inhibition of isoenzyme III
Cu2+
-
1.0 mM, 82% inhibition, levamisole-insensitive alkaline phosphatase activity; 1.0 mM, almost complete inhibition, levamisole-sensitive alkaline phosphatase activity
Cys
-
uncompetitive inhibition of phosphatase activity, mixed-competitive inhibition of inorganic pyrophosphatase activity. Inorganic pyrophosphatase activity is inhibited more than phosphatase activity. Ca2+ and Mg2+ ion concentrations may regulate this inhibition
EDTA
-
optimal reactivation by Zn2+ or Co2+. The Zn2+-reactivated enzyme is stable, the Co2+-apoenzyme is not
EDTA
0.01 mM, complete inhibition. Ca2+ is the best metal ion to reconstitute enzyme activity, followed by Co2+, Ni2+, Mn2+, and Mg2+. Zn2+, in contrast, failed to restore enzyme activity
EDTA
-
90% inhibition at 1 mM and 25°C, complete inhibition at 0.1 mM EDTA and 90°C
EDTA
-
inactivation of the native, but not of the recombinant enzyme, inhibition of the native enzyme is reversible by divalent metal ions, best effect with Co2+
F-
-
1 mM NaF, 74% inhibition of isoenzyme I, 15% inhibition of isoenzyme II
F-
-
50 mM KF, 13% inhibition of p-nitrophenyl phosphate hydrolysis, 50% inhibition of dephosphorylation of P-labelled histones
glycerol
-
concentrations of 10%, 20% and 40% inhibit the activity by 35%, 60%, and 90%
L-homoarginine
-
marked inhibition of the liver enzyme at concentrations which produce only slight inhibition of placental enzyme
L-homoarginine
-
powerful inhibitor of the bone/liver/kidney isoenzyme and for the osteosarcoma cell enzyme
L-leucine
-
allozyme D is highly sensitive and shows uncompetitive inhibition, allozymes S and F are less sensitive, allozymes SD and FD, mixed type, respond in an intermediate fashion to inhibition
L-Phe-Gly-Gly
-
marked inhibition of the placental enzyme at concentrations which produce only slight inhibition of liver enzyme
L-phenylalanine
-
the P2 isoenzyme is more sensitive to L-phenylalanine than P1
L-phenylalanine
10 mM, 100% inhibition; 10 mM, 100% inhibition; 10 mM, 37% inhibition; 10 mM, 37% inhibition, bone isoenzyme; 10 mM, 62% inhibition, isoenzyme rTI2A; 10 mM, 70% inhibition, isoenzyme rTI2B
levamisole
-
complete inhibition of the seminal plasma enzyme at 4.2 mM
levamisole
-
10 mM, 94% inhibition of p-nitrophenyl phosphate hydrolysis, 82% inhibition of dephosphorylation of P-labelled histones
levamisole
-
inhibits brush border membrane enzyme activity in the upper villus but is less effective in the middle villus and has no effect on alkaline phosphatase activity in the mucus gel
levamisole
-
hydrolysis of pyrophosphate by rat aortic rings is inhibited about half by the nonspecific alkaline phosphatase inhibitor levamisole. Hydrolysis is increased in aortic rings from uremic rats and all of this increase is inhibited by levamisole
Mn2+
-
1 mM 90% inhibition of isoenzyme I, 64% inhibition of isoenzyme II, 39% inhibition of isoenzyme III
Phe
-
marked inhibition of the placental enzyme at concentrations which produce only slight inhibition of liver enzyme
Phe
-
20 mM, 82-99% inhibition of the soluble enzyme form, 68-95% inhibition of the particulate enzyme form
phosphate
-
1 mM Na2HPO4, 74% inhibition of isoenzyme I, 15% inhibition of isoenzyme II, 2% inhibition of isoenzyme III; competitive
phosphate
hydrolytic activity decreases by 50% and 90%, respectively, in the presence of 100mM and 300mM phosphate, respectively
thioglycolic acid
-
combined treatment with thioglycolic acid, 0.175%, and 6 M urea leads to reduction of disulfide bonds, loss of activity and separation into subunits
Urea
-
combined treatment with thioglycolic acid, 0.175%, and 6 M urea leads to reduction of disulfide bonds, loss of activity and separation into subunits
Urea
-
reversible inactivation. At low concentrations of urea, the first detected alteration in properties is an increase in the activity of the enzyme. This is followed by inactivation and the release of half of the zinc content when the amount of urea reaches levels of 2 M. Intrinsic tryptophan fluorescence and circular dichroism ellipticity change in the range 2.5 to 8 M urea, signalling dimer dissociation, followed by one major monomer unfolding transition at 6-8 M urea as indicated by ANS fluorescence and KI fluorescence quenching
Urea
3 mM, 100% inhibition; 3 mM, 100% inhibition; 3 mM, 68% inhibition, bone isoenzyme; 3 mM, 70% inhibition, isoenzyme rTI2B; 3 mM, 71% inhibition; 3 mM, 80% inhibition, isoenzyme rTI2A
vanadate
-
1 mM, 22% inhibition of alkaline phosphatase grown in high phosphate medium
Zn2+
-
mutant H412Y in presence of a phosphoryl group acceptor and Zn2+ at 0.1 mM
additional information
all compounds synthesized possess moderate toxicity toward red blood cell membranes
-
additional information
-
iodoacetamide and NaN3 at 2-10 mM concentration have no effect on activity
-
additional information
Zn2+ and Mg2+ do not affect the mutant T59R enzyme
-
additional information
-
Zn2+ and Mg2+ do not affect the mutant T59R enzyme
-
additional information
enzyme is resistant to urea and dithioreitol
-
additional information
-
enzyme is resistant to urea and dithioreitol
-
additional information
-
no inhibition at 10 mM by L-phenylalanine at 10 mM for all three isozymes
-
additional information
-
with increase in concentration of the inhibitor complexes from 0.005 to 0.04 mM, an increase in Km value is observed. Each of the inhibitors serves as a mixed type of inhibitor of ALP, combining competitive and noncompetitive modes of inhibition
-
additional information
A0A196MRA0
not inhibitory: urea and Triton X-100
-
additional information
not inhibitory: ertapenem, meropenem, ampicillin or penicillin G
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
albumin
-
3fold stimulation of hydrophilic enzyme, slight stimulation of amphiphilic enzyme
-
anions
-
required for maximal activity in the order of decreasing effectiveness: Cl-, Br-, NO3-, ClO4-, SCN-
-
beta-estradiol
-
concentration dependent activation of alkaline phosphatase grown in low phosphate medium
cholesterol
-
concentration dependent activation of alkaline phosphatase grown in low phosphate medium
diethanolamine
-
highly activates BIALP. Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
L-homoarginine
-
5 mM, activation of alkaline phosphatase grown in high phosphate medium to 186% of the control value, alkaline phosphatase grown in low phosphate medium is activated to 166% of control
L-Leu
-
5 mM, activation of alkaline phosphatase grown in high phosphate medium to 155% of the control value
L-Phe
-
5 mM, activation of alkaline phosphatase grown in high phosphate medium to 168% of the control value
levamisole
-
1 mM, activation of alkaline phosphatase grown in high phosphate medium to 122% of the control value
N-Methylethanolamine
-
highly activates BIALP. Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
phosphatidylserine
-
1fold stimulation of amphiphilic enzyme form, 3fold stimulation of hydrophilic enzyme form
progesterone
-
concentration dependent activation of alkaline phosphatase grown in low phosphate medium
sodium glutamate
-
sodium glutamate promotes enzyme activity at up to 200 mM
triethanolamine
-
highly activates BIALP. Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
NaCl
Thermus sp. NTU-237
A0A1B2YKT4
the highest enzyme activity is observed when 100 mM NaCl is added to the assay reaction
NaCl
-
NaCl increases the activity and stability of the enzyme. The effect is pH-dependent in the range of pH 7.0-10.0. The relative increase in activity induced by addition of NaCl is 4fold greater at pH 7.0-8.0 than at pH 9.8. Changing the pH from 8.0 to 10.5 gradually decreases the ionic effect to near no effect at pH 10.5
Tris
-
activation at 0.2 M, increases with increasing concentration to a plateau
Tris
dephosphorylation of substrate is doubled when the Tris concentration in the reaction buffer is increased from 20 mM to 500 mM
Tris
-
activation at 0.2 M, increases with increasing concentration to a plateau
Zn2+
-
stimulation of mutant enzymes, in presence or absence of a phosphoryl group acceptor in the reaction, except for mutnat H412Y, whose activity is reduced in presence of phosphoryl group acceptor and 0.1 mM Zn2+
additional information
Zn2+ and Mg2+ do not affect the mutant T59R enzyme
-
additional information
-
Zn2+ and Mg2+ do not affect the mutant T59R enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01 - 0.177
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
0.037 - 0.1159
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
0.12
pyridoxal 5'-phosphate
-
allozyme D, pH 7.5, 37°C, in presence of Mg2+ and Zn2+
0.01
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
-
-
0.085
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
-
-
0.177
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
-
-
0.037
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
layer-by-layer single-stack, immobilized ALP
0.04
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
immobilized ALP
0.04
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
direct physical adsorption, immobilized ALP
0.05
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
free ALP
0.1058
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
layer-by-layer multi-stack, immobilized ALP
0.114
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
glutaraldehyde X-link DAH, immobilized ALP
0.1159
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
glutaraldehyde X-link, immobilized ALP
0.00000001
4-nitrophenyl phosphate
-
Vmax (mmol/min mg of protein): 1.8 (dimer), 0.42 (tetramer)
0.0005
4-nitrophenyl phosphate
mutant enzyme E332Y, at pH 8.0 and 25°C
0.0021
4-nitrophenyl phosphate
mutant enzyme R166S/E322Y/K328A, at pH 8.0 and 25°C
0.0022
4-nitrophenyl phosphate
mutant enzyme E322Y/K328A, at pH 8.0 and 25°C
0.0024
4-nitrophenyl phosphate
mutant enzyme D153A/K328A, at pH 8.0 and 25°C
0.0026
4-nitrophenyl phosphate
mutant enzyme D153A, at pH 8.0 and 25°C
0.0035
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.0036
4-nitrophenyl phosphate
mutant enzyme D101A, at pH 8.0 and 25°C
0.0048
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A, at pH 8.0 and 25°C
0.005
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.005
4-nitrophenyl phosphate
mutant enzyme R166S, at pH 8.0 and 25°C
0.0051
4-nitrophenyl phosphate
mutant Y222P, presence of 0.5 M NaCl, pH 8, 10°C
0.0053
4-nitrophenyl phosphate
mutant enzyme R166S/D153A, at pH 8.0 and 25°C
0.0054
4-nitrophenyl phosphate
mutant enzyme K328A, at pH 8.0 and 25°C
0.0054
4-nitrophenyl phosphate
mutant Y423F, presence of 0.5 M NaCl, pH 8, 10°C
0.0062
4-nitrophenyl phosphate
mutant enzyme D101A/D153A, at pH 8.0 and 25°C
0.0073
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.0073
4-nitrophenyl phosphate
mutant K422L, presence of 0.5 M NaCl, pH 8, 10°C
0.0073
4-nitrophenyl phosphate
mutant K422E, presence of 0.5 M NaCl, pH 8, 10°C
0.0079
4-nitrophenyl phosphate
wild-type, presence of 0.5 M NaCl, pH 8, 10°C
0.0084
4-nitrophenyl phosphate
mutant enzyme D101A/R166S, at pH 8.0 and 25°C
0.0094
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.0095
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.0097
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.011
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.011
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/K328A, at pH 8.0 and 25°C
0.011
4-nitrophenyl phosphate
mutant K422L/Y423F, presence of 0.5 M NaCl, pH 8, 10°C
0.012
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/E322Y, at pH 8.0 and 25°C
0.0128
4-nitrophenyl phosphate
mutant A221D, presence of 0.5 M NaCl, pH 8, 10°C
0.0145
4-nitrophenyl phosphate
-
pH 8, 25°C, in the presence of phosphate acceptor (1 M Tris-HCl buffer)
0.0176
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.0211
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.0218
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant wild-type enzyme
0.0221
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.027
4-nitrophenyl phosphate
mutant enzyme R166S/E322Y, at pH 8.0 and 25°C
0.02982
4-nitrophenyl phosphate
single-chain Fv antibody fusion protein
0.0374
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.052
4-nitrophenyl phosphate
mutant enzyme D153A/E322Y, at pH 8.0 and 25°C
0.057
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.0597
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.06
4-nitrophenyl phosphate
-
10°C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
0.063
4-nitrophenyl phosphate
mutant enzyme R166S/K328A, at pH 8.0 and 25°C
0.0691
4-nitrophenyl phosphate
-
mutant D434E, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.078
4-nitrophenyl phosphate
mutant enzyme D101A/E322Y/K328A, at pH 8.0 and 25°C
0.082
4-nitrophenyl phosphate
-
pH 9.5, 37°C, Vmax: 0.96 nmol/min/mg enzyme, CIAP immobilized enzyme reactor (in excellent agreement with a Km value of calf ALP enzyme using a 96-well microplate reader)
0.087
4-nitrophenyl phosphate
pH 9.5, 50°C, Vmax: 0.049 micromol/min/mg
0.12
4-nitrophenyl phosphate
-
37°C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
0.14
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/K328A, at pH 8.0 and 25°C
0.14
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.15
4-nitrophenyl phosphate
mutant enzyme D101A/E322Y, at pH 8.0 and 25°C
0.16
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.18
4-nitrophenyl phosphate
-
57°C, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.198
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.2
4-nitrophenyl phosphate
-
37°C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.2
4-nitrophenyl phosphate
-
37°C, pH 9.5, mutant os-1 enzyme, without MgCl2
0.22
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.23
4-nitrophenyl phosphate
-
37°C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.27
4-nitrophenyl phosphate
-
37°C, pH 9.5, wild-type enzyme, without MgCl2
0.29
4-nitrophenyl phosphate
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
0.29
4-nitrophenyl phosphate
-
fusion protein with ZZ protein, pH not specified in the publication, temperature not specified in the publication
0.31
4-nitrophenyl phosphate
-
conjugate between enzyme and ZZ protein, pH not specified in the publication, temperature not specified in the publication
0.35
4-nitrophenyl phosphate
mutant enzyme D153A/E322Y/K328A, at pH 8.0 and 25°C
0.38
4-nitrophenyl phosphate
-
presence of FeCl3, pH 8.5, 45°C
0.44
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/E322Y, at pH 8.0 and 25°C
0.85
4-nitrophenyl phosphate
-
37°C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
1.37
4-nitrophenyl phosphate
-
pH not specified, 37°C, Vmax: 0.011 mM/min, in the presence of 0.8 M NaN3
1.91
4-nitrophenyl phosphate
-
pH 9.5, 37°C, Vmax: 0.029 mM/min, in the presence of 0.8 M KNO3
2.44
4-nitrophenyl phosphate
-
pH 10.5, 37°C, enzyme immobilized by phosphatase-polyresorcinol complex
2.52
4-nitrophenyl phosphate
-
pH 9.5, 37°C, Vmax: 0.023 mM/min, in the presence of 0.8 M KCl
2.54
4-nitrophenyl phosphate
-
pH 10, 37°C, Vmax: 0.018 mM/min, in the presence of 0.8 M NaAc
2.73
4-nitrophenyl phosphate
-
pH 9.25, 37°C, Vmax: 0.02 mM/min, in the presence of 0.8 M KPF6
3.43
4-nitrophenyl phosphate
-
pH 9.25, 37°C, Vmax: 0.021 mM/min, in the presence of 0.8 M NaNO3
4.4
4-nitrophenyl phosphate
-
pH 9, 37°C, Vmax: 0.016 mM/min, in the presence of 0.8 M NaBF4
4.42
4-nitrophenyl phosphate
-
pH 9.5, 37°C, Vmax: 0.028 mM/min, in the presence of 0.8 M NaCl
4.59
4-nitrophenyl phosphate
-
pH 9.8, recombinant enzyme expressed in Tn-5B1-4 cells
4.7
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 384 mM NaCl, without Mn2+
4.9
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, without Mn2+
6.76
4-nitrophenyl phosphate
-
pH 9.8, recombinant enzyme expressed in Sf-9 cells
6.87
4-nitrophenyl phosphate
-
pH 9, 37°C, Vmax: 0.022 mM/min, in the presence of 0.8 M Na2SO4
7.32
4-nitrophenyl phosphate
-
pH not specified, 37°C, Vmax: 0.019 mM/min, in the presence of 0.8 M Na citrate
8.6
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, 2.5 mM Mn2+
9
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 384 mM K+, 2.5 mM MnCl2
9.7
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM K+, 2.5 mM MnCl2
11.6
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 384 mM NaCl, 2.5 mM Mn2+
13.9
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 192 mM NaCl, 2.5 mM Mn2+
14.4
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, 5 mM Mn2+
16.7
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 192 mM NaCl, without Mn2+
16.8
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, 8 mM Mn2+
25.4
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 192 mM K+, 2.5 mM MnCl2
0.0094
p-nitrophenyl phosphate
-
wild type enzyme, in absence of a phosphate acceptor
0.02124
p-nitrophenyl phosphate
-
wild type enzyme, in presence of a phosphate acceptor
0.037
p-nitrophenyl phosphate
-
pH 9.2, absence of divalent metal ions
0.05972
p-nitrophenyl phosphate
-
mutant enzyme D369N, in presence of a phosphate acceptor
0.176
p-nitrophenyl phosphate
-
mutant enzyme D369N, in absence of a phosphate acceptor
2.941
p-nitrophenyl phosphate
-
mutant enzyme D369A, in absence of a phosphate acceptor
additional information
4-nitrophenyl phosphate
-
the Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
additional information
additional information
-
kinetic characterization of the homodimeric complementation mutants, and heterodimeric hybrid formation
-
additional information
additional information
-
kinetics of other allozymes of PALP
-
additional information
additional information
-
kinetics at several temperatures and pH-value combinations
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
92
pyridoxal 5'-phosphate
-
allozyme D, pH 7.5, 37°C, in presence of Mg2+ and Zn2+
0.000029
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.000057
4-nitrophenyl phosphate
mutant enzyme R166S/E322Y/K328A, at pH 8.0 and 25°C
0.00021
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant mutant T59R
0.00024
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.00032
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/E322Y, at pH 8.0 and 25°C
0.00073
4-nitrophenyl phosphate
mutant enzyme D153A/E322Y/K328A, at pH 8.0 and 25°C
0.00089
4-nitrophenyl phosphate
mutant enzyme D101A/E322Y/K328A, at pH 8.0 and 25°C
0.00096
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.0014
4-nitrophenyl phosphate
mutant enzyme D153A/E322Y, at pH 8.0 and 25°C
0.0026
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/K328A, at pH 8.0 and 25°C
0.0034
4-nitrophenyl phosphate
mutant enzyme E322Y/K328A, at pH 8.0 and 25°C
0.0083
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/E322Y, at pH 8.0 and 25°C
0.016
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.016
4-nitrophenyl phosphate
mutant enzyme R166S/K328A, at pH 8.0 and 25°C
0.027
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.037 - 0.23
4-nitrophenyl phosphate
-
37°C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.042
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.052
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.059
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.061
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/K328A, at pH 8.0 and 25°C
0.067
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.07
4-nitrophenyl phosphate
mutant enzyme R166S/D153A, at pH 8.0 and 25°C
0.083
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A, at pH 8.0 and 25°C
0.1
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.32
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.39
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.55
4-nitrophenyl phosphate
-
10°C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
1.1
4-nitrophenyl phosphate
mutant enzyme D153A/K328A, at pH 8.0 and 25°C
1.6
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/K328A, at pH 8.0 and 25°C
2.2
4-nitrophenyl phosphate
mutant enzyme D101A/D153A, at pH 8.0 and 25°C
2.3
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant wild-type enzyme
2.4
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
3 - 6
4-nitrophenyl phosphate
mutant enzyme D101A, at pH 8.0 and 25°C
3.8
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
4.2
4-nitrophenyl phosphate
mutant enzyme D101A/R166S, at pH 8.0 and 25°C
4.6
4-nitrophenyl phosphate
mutant enzyme D101A/E322Y, at pH 8.0 and 25°C
5.8
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
14.67
4-nitrophenyl phosphate
-
10°C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
20 - 50
4-nitrophenyl phosphate
-
57°C, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
29.9
4-nitrophenyl phosphate
-
pH 8, 25°C, in the presence of phosphate acceptor (1 M Tris-HCl buffer)
44.4
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
65.6
4-nitrophenyl phosphate
-
mutant D434E, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
74.7
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant wild-type enzyme
77.4
4-nitrophenyl phosphate
-
37°C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
78.83
4-nitrophenyl phosphate
-
37°C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
80.5
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
87.83
4-nitrophenyl phosphate
-
57°C, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
88
4-nitrophenyl phosphate
mutant K422E, presence of 0.5 M NaCl, pH 8, 10°C
113.6
4-nitrophenyl phosphate
single-chain Fv antibody fusion protein
140
4-nitrophenyl phosphate
mutant K422L/Y423F, presence of 0.5 M NaCl, pH 8, 10°C
153.9
4-nitrophenyl phosphate
-
37°C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
223
4-nitrophenyl phosphate
mutant K422L, presence of 0.5 M NaCl, pH 8, 10°C
224
4-nitrophenyl phosphate
mutant Y423F, presence of 0.5 M NaCl, pH 8, 10°C
285
4-nitrophenyl phosphate
-
conjugate between enzyme and ZZ protein, pH not specified in the publication, temperature not specified in the publication
304
4-nitrophenyl phosphate
mutant A221D, presence of 0.5 M NaCl, pH 8, 10°C
328
4-nitrophenyl phosphate
mutant Y222P, presence of 0.5 M NaCl, pH 8, 10°C
356
4-nitrophenyl phosphate
wild-type, presence of 0.5 M NaCl, pH 8, 10°C
361
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant H135E/G149D
370
4-nitrophenyl phosphate
-
fusion protein with ZZ protein, pH not specified in the publication, temperature not specified in the publication
378
4-nitrophenyl phosphate
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
1443
4-nitrophenyl phosphate
-
37°C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
16230
4-nitrophenyl phosphate
-
37°C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
4200
6,8-difluoro-4-methylumbelliferyl phosphate
-
mutant G168K, pH 9.3, temperature not specified in the publication
4200
6,8-difluoro-4-methylumbelliferyl phosphate
-
mutant G168R, pH 9.3, temperature not specified in the publication
0.01
p-nitrophenyl phosphate
-
mutant enzyme D369A, in absence of a phosphate acceptor
0.4
p-nitrophenyl phosphate
-
mutant enzyme D369N, in absence of a phosphate acceptor
80.5
p-nitrophenyl phosphate
-
wild type enzyme, in presence of a phosphate acceptor
230
p-nitrophenyl phosphate
-
mutant enzyme D369N, in presence of a phosphate acceptor
additional information
4-nitrophenyl phosphate
-
turnover number is 3300000/s, pH 10.3, 40°C
additional information
additional information
kcat/KM (1/Msec) wild-type: 140000, mutant R166K: 20, mutant R166S: 24
-
additional information
additional information
-
kcat/KM (1/Msec) wild-type: 140000, mutant R166K: 20, mutant R166S: 24
-
additional information
additional information
wild-type enzyme: kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 33000000, (3-nitrobenzyl phosphate): 18000000, (methyl phosphate): 1200000, (methyl 4-nitrophenyl phosphate): 18, (bis-4-nitrophenyl phosphate): 0.05, (4-nitrophenyl sulfate): 0.01
-
additional information
Phenyl phosphate
-
turnover number is 2540000/s, pH 10.3, 40°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/E322Y/K328A, at pH 8.0 and 25°C
0.00017
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.00039
4-nitrophenyl phosphate
mutant enzyme R166S/E322Y/K328A, at pH 8.0 and 25°C
0.00094
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/E322Y, at pH 8.0 and 25°C
0.0011
4-nitrophenyl phosphate
mutant enzyme D101A/E322Y/K328A, at pH 8.0 and 25°C
0.0016
4-nitrophenyl phosphate
mutant enzyme R166S/E322Y, at pH 8.0 and 25°C
0.002
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.0031
4-nitrophenyl phosphate
mutant enzyme D101A/E322Y, at pH 8.0 and 25°C
0.0044
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.013
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/E322Y, at pH 8.0 and 25°C
0.019
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/E322Y, at pH 8.0 and 25°C
0.24
4-nitrophenyl phosphate
mutant enzyme R166S/K328A, at pH 8.0 and 25°C
0.28
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/K328A, at pH 8.0 and 25°C
0.32
4-nitrophenyl phosphate
mutant enzyme D153A/E322Y/K328A, at pH 8.0 and 25°C
0.42
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/E322Y, at pH 8.0 and 25°C
1.5
4-nitrophenyl phosphate
mutant enzyme E322Y/K328A, at pH 8.0 and 25°C
2.3
4-nitrophenyl phosphate
mutant enzyme D153A/E322Y, at pH 8.0 and 25°C
3.6
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/K328A, at pH 8.0 and 25°C
5.5
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/K328A, at pH 8.0 and 25°C
13
4-nitrophenyl phosphate
mutant enzyme R166S/D153A, at pH 8.0 and 25°C
20
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A, at pH 8.0 and 25°C
28
4-nitrophenyl phosphate
mutant enzyme D101A/K328A, at pH 8.0 and 25°C
58
4-nitrophenyl phosphate
mutant enzyme D101A/R166S, at pH 8.0 and 25°C
120
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/K328A, at pH 8.0 and 25°C
330
4-nitrophenyl phosphate
mutant enzyme D101A/D153A, at pH 8.0 and 25°C
440
4-nitrophenyl phosphate
mutant enzyme D153A/K328A, at pH 8.0 and 25°C
12000
4-nitrophenyl phosphate
mutant K422E, presence of 0.5 M NaCl, pH 8, 10°C
13000
4-nitrophenyl phosphate
mutant K422L/Y423F, presence of 0.5 M NaCl, pH 8, 10°C
20000
4-nitrophenyl phosphate
mutant A221D, presence of 0.5 M NaCl, pH 8, 10°C
31000
4-nitrophenyl phosphate
mutant K422L, presence of 0.5 M NaCl, pH 8, 10°C
41000
4-nitrophenyl phosphate
mutant Y423F, presence of 0.5 M NaCl, pH 8, 10°C
45000
4-nitrophenyl phosphate
wild-type, presence of 0.5 M NaCl, pH 8, 10°C
64000
4-nitrophenyl phosphate
mutant Y222P, presence of 0.5 M NaCl, pH 8, 10°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00036
2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)-N-(3-(trifluoromethyl)phenyl)acetamide
pH 9.5, 37°C
0.0032
2-([(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)sulfonyl]amino)-N-(2,5-dimethylphenyl)acetamide
pH not specified in the publication, temperature not specified in the publication
0.0089
arsenate
-
pH 9.5, 37°C, ALP immobilized capillary electrophoresis, Ki value is close to the Ki values obtained by the standard spectrophotometric assay
0.00241
phosphate
-
pH 9.5, 37°C, ALP immobilized capillary electrophoresis, Ki value is close to the Ki values obtained by the standard spectrophotometric assay
0.423
phosphate
-
pH 10.5, 37°C, enzyme immobilized by phosphatase-polyresorcinol complex
0.05
theophylline
-
pH 9.5, 37°C, ALP immobilized capillary electrophoresis, Ki value is close to the Ki values obtained by the standard spectrophotometric assay
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004311
(2E)-1-(3,5-dibromo-2-hydroxyphenyl)-3-(furan-2-yl)prop-2-en-1-one
Bos taurus
pH 9.5, 37°C
0.012563
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-(2,4-dimethylphenyl)prop-2-en-1-one
Bos taurus
pH 9.5, 37°C
0.006967
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-(3-methoxy-4-propoxyphenyl)prop-2-en-1-one
Bos taurus
pH 9.5, 37°C
0.007547
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-(4-fluorophenyl)prop-2-en-1-one
Bos taurus
pH 9.5, 37°C
0.003141
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-(4-methoxyphenyl)prop-2-en-1-one
Bos taurus
pH 9.5, 37°C
0.008453
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-(thiophen-2-yl)prop-2-en-1-one
Bos taurus
pH 9.5, 37°C
0.003023
(2E)-1-(5-chloro-2-hydroxy-3-nitrophenyl)-3-[4-(dimethylamino)phenyl]prop-2-en-1-one
Bos taurus
pH 9.5, 37°C
0.005543
(2E)-2-[4-(benzyloxy)-[3-methoxyphenyl]methylidene]-6-chloro-4-nitro-1-benzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
-
0.006231
(2E)-3-(4-chlorophenyl)-1-(3,5-dibromo-2-hydroxyphenyl)prop-2-en-1-one
Bos taurus
pH 9.5, 37°C
0.009563
(2E)-3-[4-(benzyloxy)-3-methoxyphenyl]-1-(5-chloro-2-hydroxy-3-nitrophenyl)prop-2-en-1-one
Bos taurus
pH 9.5, 37°C
0.002163
(2E)-4,6-dibromo-2-[(4-chlorophenyl)methylidene]-1-benzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
0.004657
(2E)-4,6-dibromo-2-[(furan-2-yl)methylidene]-1-benzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
0.005786
(2E)-4,6-dibromo-2-[[4-(trifluoromethyl)phenyl]methylidene]-1-benzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
0.004876
(2E)-6-chloro-2-(4-fluorobenzylidene)-4-nitrobenzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
-
0.001055
(2E)-6-chloro-2-(4-methoxybenzylidene)-4-nitrobenzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
-
0.001154
(2E)-6-chloro-2-[(2,4-dimethylphenyl)methylidene]-4-nitro-1-benzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
0.002326
(2E)-6-chloro-2-[(3-methoxy-4-propoxyphenyl)methylidene]-4-nitro-1-benzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
0.002132
(2E)-6-chloro-2-[(4-chlorophenyl)methylidene]-4-nitro-1-benzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
0.002146
(2E)-6-chloro-2-[[4-(dimethylamino)phenyl]methylidene]-4-nitro-1-benzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
0.005876
(2E)-6-chloro-4-nitro-2-[(thiophen-2-yl)methylidene]-1-benzofuran-3(2H)-one
Bos taurus
pH 9.5, 37°C
0.00106 - 0.00398
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
0.00067
(E)-N'-(4'-chlorobenzylidene)isonicotinohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.0058
1-(3,4-dihydroxyphenyl)-2-(5,6-dimethyl-1H-benzimidazol-1-yl)ethanone
Homo sapiens
-
-
0.0067
1-(3,4-dihydroxyphenyl)-2-[(4-methyl-5-phenyl-4H-1,2,4-triazol-3-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.002 - 0.008
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
0.00109 - 0.00651
1-(4-hydroxy, 3-methoxybenzylidene)-2-(4-tertbutylthiazol-2-yl)hydrazine
0.00349
1-(4-tert-butylthiazol-2-yl)-2-(furan-2-ylmethylene)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000488
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-ethylpiperazine
Bos taurus
-
0.000828
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-methylpiperazine
Bos taurus
-
0.000344
2,4-dichloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.0103
2,5-dimethoxy-N-(pyridin-3-yl)benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.0088
2,6-diamino-1-benzyl-4-(2,3,4-trimethoxyphenyl)-1,4-dihydropyridine-3,5-dicarbonitrile
Homo sapiens
pH 9.5, 37°C
0.00225
2,6-diamino-1-benzyl-4-(3-hydroxy-2-methoxyphenyl)-1,4-dihydropyridine-3,5-dicarbonitrile
Homo sapiens
pH 9.5, 37°C
0.00132
2,6-diamino-1-benzyl-4-(naphthalen-2-yl)-1,4-dihydropyridine-3,5-dicarbonitrile
Homo sapiens
pH 9.5, 37°C
0.00122
2-((3-(1H-imidazol-1-yl)propyl)amino)-6-amino-4-(4-ethoxyphenyl)pyridine-3,5-dicarbonitrile
Homo sapiens
pH 9.5, 37°C
0.00042
2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)-N-(3-(trifluoromethyl)phenyl)acetamide
Bos taurus
pH 9.5, 37°C
0.001793
2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)-N-(4-bromophenyl)acetamide
Bos taurus
pH 9.5, 37°C
0.008348
2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)-N-(4-chlorophenyl)acetamide
Bos taurus
pH 9.5, 37°C
0.003765
2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)-N-phenylacetamide
Bos taurus
pH 9.5, 37°C
0.00202 - 0.00222
2-(1-methylhydrazenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00452 - 0.1
2-(2-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00348 - 0.1
2-(2-methoxyphenyl)-7- trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00054 - 0.00175
2-(3,4-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00076 - 0.00115
2-(3,5-di-methoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00046 - 0.00052
2-(3,5-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00056 - 0.00112
2-(3-cyanophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00052 - 0.00068
2-(3-fluoromethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00074 - 0.00139
2-(3-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00038 - 0.00044
2-(3-methoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00048 - 0.00062
2-(3-nitrophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00112 - 0.00167
2-(3-phenylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00033 - 0.00071
2-(4-aminophenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00079 - 0.00093
2-(4-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00158 - 0.00202
2-(4-ethoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00455 - 0.1
2-(4-ethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00198 - 0.0315
2-(4-i-propylphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00028 - 0.00048
2-(4-methoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00036 - 0.00106
2-(4-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00024 - 0.1
2-(4-trifluoromethoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.000375
2-(4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]piperazin-1-yl)ethanol
Bos taurus
-
0.00054
2-([(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)sulfonyl]amino)-N-(2,5-dimethylphenyl)acetamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.00029 - 0.00089
2-allylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.003458
2-chloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.000322
2-cyano-6-methoxy-N-(pyridin-3-yl)benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.00153 - 0.00463
2-di-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.001233
2-isopropyl-5-methylphenyl 2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)acetate
Bos taurus
pH 9.5, 37°C
0.000896
2-methoxy-5-methyl-N-(pyridin-3-yl)benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.001233
2-methoxyphenyl 2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)acetate
Bos taurus
pH 9.5, 37°C
0.00071 - 0.00088
2-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00061 - 0.00076
2-n-pentylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00031 - 0.00144
2-n-propylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00045 - 0.00375
2-[2-(dimethylamino)ethyl]amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.0022 - 0.0048
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
0.000896
3,5-dinitro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.000127
3-(2,4-dichloro-5-fluorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000324
3-(2,4-dichloro-5-fluorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
Bos taurus
-
0.00485
3-(2,4-dichloro-5-fluorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.0001
3-(2,4-dichloro-5-fluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000056
3-(2,4-dichloro-5-fluorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000047
3-(2,4-dichlorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000051
3-(2,4-dichlorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000044
3-(2,4-dichlorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000046
3-(2,4-dichlorophenyl)-N-(2-methoxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000082
3-(2,4-dichlorophenyl)-N-(2-methylpropyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000031
3-(2,4-dichlorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000459
3-(2,4-dichlorophenyl)-N-(3-methylbutyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000035
3-(2,4-dichlorophenyl)-N-(4-hydroxybutyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000035
3-(2,4-difluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.00149
3-methoxy-2-[(pyridin-3-yl)sulfamoyl]benzamide
Mus musculus
pH and temperature not specified in the publication
0.000876
3-methoxy-N-(pyridin-3-yl)[1,1'-biphenyl]-2-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.003 - 0.0292
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
0.00049
4-(2-((6-amino-3,5-dicyano-4-(4-ethoxyphenyl)pyridine-2yl)amino)ethyl)benzene sulfonamide
Homo sapiens
pH 9.5, 37°C
0.005012
4-allyl-2-methoxyphenyl 2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)acetate
Bos taurus
pH 9.5, 37°C
0.000251
4-chloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.001547
4-fluoro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.004844
4-formyl-2-methoxyphenyl 2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)acetate
Bos taurus
pH 9.5, 37°C
0.003291
4-methoxy-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.0027219
4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)-methyl]-N-(2-methylphenyl)benzamide
Bos taurus
pH 9.5, 37°C
0.0009666
4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)-methyl]-N-(3-methylphenyl)benzamide
Bos taurus
pH 9.5, 37°C
0.0028069
4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)-methyl]-N-(4-methylphenyl)benzamide
Bos taurus
pH 9.5, 37°C
0.00417
5-chloro-2-methoxy-N-(pyridin-3-yl)benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000178
5-chloro-2-methoxy-N-[5-(2-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.00016
5-chloro-2-methoxy-N-[5-(3-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000023
5-chloro-2-methoxy-N-[5-(4-methoxyphenyl)pyridin-3-yl]benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000147
5-chloro-2-methoxy-N-[5-(4-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000671
5-chloro-2-methoxy-N-[5-(4-methylpiperazine-1-carbonyl)pyridin-3-yl]benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000198
5-chloro-N-[5-(4-chlorophenyl)pyridin-3-yl]-2-methoxybenzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000183
5-methyl-3-[3-[3-(trifluoromethyl)phenyl]prop-2-yn-1-yl]oxolan-2-one
Mus musculus
pH and temperature not specified in the publication
0.000014
5-[(5-bromo-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000193
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-ethylpyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000109
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-methylpyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.00031
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-phenylpyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000016
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000134
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxylic acid
Mus musculus
pH and temperature not specified in the publication
0.000019
5-[(5-fluoro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000131
5-[[2-methoxy-5-(trifluoromethoxy)benzene-1-sulfonyl]amino]pyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000432
5-[[5-chloro-2-(trifluoromethoxy)benzene-1-sulfonyl]amino]pyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000084
6-(1-benzofuran-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
Mus musculus
pH and temperature not specified in the publication
0.000043
6-(5-nitro-1-benzothiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
Mus musculus
pH and temperature not specified in the publication
0.000038
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
Mus musculus
pH and temperature not specified in the publication
0.192 - 0.408
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
0.004801
benzo[d][1,3]dioxol-5-yl 2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)acetate
Bos taurus
pH 9.5, 37°C
0.00151
methyl 3-methoxy-2-[(pyridin-3-yl)sulfamoyl]benzoate
Mus musculus
pH and temperature not specified in the publication
0.000065
methyl 5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxylate
Mus musculus
pH and temperature not specified in the publication
0.00144
N'-[(Z)-(2-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00246
N'-[(Z)-(pyridin-4-yl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.004256
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)acetamide
Bos taurus
-
at pH 9.5 and 37°C
0.001636
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)butyramide
Bos taurus
-
at pH 9.5 and 37°C
0.000492
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)heptanamide
Bos taurus
-
at pH 9.5 and 37°C
0.001704
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)octanamide
Bos taurus
-
at pH 9.5 and 37°C
0.000052
N-(2,3-dimethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
Bos taurus
pH 9.5, 37°C
0.0004785
N-(2,4-dimethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
Bos taurus
pH 9.5, 37°C
0.0003205
N-(2,6-dimethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
Bos taurus
pH 9.5, 37°C
0.0003806
N-(2-ethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
Bos taurus
pH 9.5, 37°C
0.000005 - 0.000026
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
0.000134
N-(2-hydroxyethyl)-3-(2,4,5-trifluorophenyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.0002063
N-(3,4-dimethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
Bos taurus
pH 9.5, 37°C
0.0000456
N-(3,5-dimethylphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
Bos taurus
pH 9.5, 37°C
0.00182
N-(3-cyanophenyl)-3-([(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)sulfonyl]amino)propanamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.0000676
N-(3-ethoxyphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
Bos taurus
pH 9.5, 37°C
0.0000427
N-(4-ethoxyphenyl)-4-[([5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazol-2-yl]sulfanyl)methyl]benzamide
Bos taurus
pH 9.5, 37°C
0.00012
N-([3,3'-bipyridin]-5-yl)-2,5-dimethoxybenzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000073
N-([3,3'-bipyridin]-5-yl)-5-chloro-2-methoxybenzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000073
N-([3,4'-bipyridin]-5-yl)-2,5-dimethoxybenzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000073
N-([3,4'-bipyridin]-5-yl)-5-chloro-2-methoxybenzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.002374
phenyl 2-((5-benzyl-1,3,4-oxadiazol-2-yl)thio)acetate
Bos taurus
pH 9.5, 37°C
0.00106
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00398
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00035
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00192
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.0088
1-(2,4-dihydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.028
1-(2,4-dihydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0006
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.0025
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.0086
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.0495
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.002
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
Homo sapiens
-
-
0.008
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
Homo sapiens
-
-
0.00071
1-(3,4-dimethoxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.041
1-(3,4-dimethoxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0085
1-(3-hydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0273
1-(3-hydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00212
1-(4-chlorobenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00602
1-(4-chlorobenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00109
1-(4-hydroxy, 3-methoxybenzylidene)-2-(4-tertbutylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00651
1-(4-hydroxy, 3-methoxybenzylidene)-2-(4-tertbutylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00488
1-(4-hydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00547
1-(4-hydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.028
1-(4-tert-butylthiazol-2-yl)-2-(1-phenylethylidene)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.032
1-(4-tert-butylthiazol-2-yl)-2-(1-phenylethylidene)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.025
1-(5-bromo,2-hydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.043
1-(5-bromo,2-hydroxybenzylidene)-2-(4-tert-butylthiazol-2-yl)hydrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00202
2-(1-methylhydrazenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00222
2-(1-methylhydrazenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00452
2-(2-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(2-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(2-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(2-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00348
2-(2-methoxyphenyl)-7- trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(2-methoxyphenyl)-7- trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00054
2-(3,4-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00175
2-(3,4-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00076
2-(3,5-di-methoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00115
2-(3,5-di-methoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00046
2-(3,5-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00052
2-(3,5-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00056
2-(3-cyanophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00112
2-(3-cyanophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00052
2-(3-fluoromethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00068
2-(3-fluoromethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00074
2-(3-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00139
2-(3-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00038
2-(3-methoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00044
2-(3-methoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00048
2-(3-nitrophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00062
2-(3-nitrophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00112
2-(3-phenylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00167
2-(3-phenylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00033
2-(4-aminophenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00071
2-(4-aminophenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.0049
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.0087
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.00079
2-(4-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00093
2-(4-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00158
2-(4-ethoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00202
2-(4-ethoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00455
2-(4-ethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(4-ethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00198
2-(4-i-propylphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.0315
2-(4-i-propylphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00028
2-(4-methoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00048
2-(4-methoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00036
2-(4-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00106
2-(4-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00024
2-(4-trifluoromethoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(4-trifluoromethoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00029
2-allylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00089
2-allylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00153
2-di-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00463
2-di-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00071
2-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00088
2-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00061
2-n-pentylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00076
2-n-pentylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00031
2-n-propylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00144
2-n-propylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00021
2-phenyl-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00043
2-phenyl-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00045
2-[2-(dimethylamino)ethyl]amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00375
2-[2-(dimethylamino)ethyl]amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.0022
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
Homo sapiens
-
-
0.0048
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
Homo sapiens
-
-
0.8
3-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C, value higher than 0.8 mM
0.8
3-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C, value higher than 0.8 mM
0.003
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
Homo sapiens
-
-
0.0292
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
Homo sapiens
-
-
0.8
6-(thiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C, value higher than 0.8 mM
0.8
6-(thiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C, value higher than 0.8 mM
0.26
6-(thiophen-2-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C
0.331
6-(thiophen-2-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C
0.192
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C
0.408
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C
0.8
6-(thiophen-3-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C, value higher than 0.8 mM
0.8
6-(thiophen-3-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C, value higher than 0.8 mM
0.042
6-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C
0.084
6-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C
0.8
6-(thiophen-3-yl)imidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C, value higher than 0.8 mM
0.8
6-(thiophen-3-yl)imidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C, value higher than 0.8 mM
0.08
L-phenylalanine
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.0802
L-phenylalanine
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
L-phenylalanine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0192
levamisole
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.0192
levamisole
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00182
N'-[(Z)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00734
N'-[(Z)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00413
N'-[(Z)-(4-bromophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00972
N'-[(Z)-(4-bromophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00226
N'-[(Z)-(4-fluorophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.0175
N'-[(Z)-(4-fluorophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00056
N'-[(Z)-(4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00174
N'-[(Z)-(4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00146
N'-[(Z)-(pyridin-3-yl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00243
N'-[(Z)-(pyridin-3-yl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.000005
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000026
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
4
phosphate
Escherichia coli
-
pH 10.5, 37°C, enzyme immobilized by phosphatase-polyresorcinol complex
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.05 - 3.62
-
isozymes in intestine segmented into 20 segments, highest activity in the apical part, lowest in the basal, overview
30.8
additional information
additional information
-
activity in different tissue and fluid samples
additional information
-
activity in pre-, and ejaculate samples and in tissue samples
additional information
-
extracellular alkaline phosphatase shows 3fold more activity with tyrosine phosphate in comparison to p-nitrophenylphosphate
additional information
-
57% of intestinal activity is retained using HPLC for separation. Increased activity is detected after cleaving ALP from the cellular membrane by GPI-specific phospholipase C
additional information
57% of intestinal activity is retained using HPLC for separation. Increased activity is detected after cleaving ALP from the cellular membrane by GPI-specific phospholipase C
additional information
-
56% of intestinal activity is retained using HPLC for separation
additional information
56% of intestinal activity is retained using HPLC for separation
additional information
-
PhoX activity is elevated 90fold within 5 h after inoculation into phosphate-free medium, whereas activity in cells resuspended in phosphate-replete medium remains almost undetectable
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
10.1
10.2
10.3
10.4
10.5
11
12
7.5
8.5
8.5 - 9.5
8.8
8.9
9 - 9.5
9.2
9.5
9.8
10
-
low-molecular weight alkaline phosphatase and high-molecular weight alkaline phosphatase, phosphomonoesterase activity
10
-
low-molecular weight alkaline phosphatase, phosphodiesterase activity, CAPS buffer
10.2
-
maximal activity of both free enzyme and enzyme immobilized by phosphatase-polyresorcinol complex
10.2
-
the pH-activity profile shows two maxima at approximately pH 9.0 and 10.2
10.5
-
hydrolysis of 8 mM p-nitrophenyl phosphate, 2-amino-2-methylpropan-1-ol hydrochloride buffer
8.5
-
five buffer systems are investigated at pH 8.5: tris, carbonate, hepes, borate, and glycine buffers, and the lowest catalytic activity of alkaline phosphatases at equal pH is observed in the borate buffer. The highest specific activity, is observed in the buffer solution of tris-(oxymethyl)-aminomethane-HCl
8.5
-
wild-type enzyme and alkaline phosphatase fused to a C-terminal region of Pseudomonas sp. MIS38 lipase
8.5
-
low-molecular weight alkaline phosphatase, phosphodiesterase activity, CHES buffer
9
-
the pH-activity profile shows two maxima at approximately pH 9.0 and 10.2
9.8
-
hydrolysis of 2 mM p-nitrophenyl phosphate, 2-amino-2-methylpropan-1-ol hydrochloride buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11 - 12.5
11.0: about 50% of maximal activity, pH 12.5: about 65% of maximal activity
5 - 10
-
activity profile of free enzyme is comparable to immobilized enzyme
6 - 12
-
the enzyme retains a high activity (more than 50%) in the pH range from pH 6.0-12.0
6 - 9
-
pH 6.0: about 30% of maximal activity, pH 9.0: about 15% of maximal activity
7 - 10
-
pH 7.0: about 20% of maximal activity, pH 10.0: about 90% of maximal activity
7 - 10.5
-
pH 7.0: about 10% of maximal activity, pH 10.5: about 35% of maximal activity
7.5 - 10.5
-
pH 7.5: about 45% of maximal activity, pH 10.5: about 30% of maximal activity
7.5 - 9.5
-
pH 7.5: about 60% of maximal activity, pH 9.5: about 65% of maximal activity, wild-type enzyme and alkaline phosphatase fused to a C-terminal region of Pseudomonas sp. MIS38 lipase
8 - 10
-
pH 8.0: about 50% of maximal activity of mutant enzyme os-1, pH 10: about 95% of maximal activity of mutant enzyme os-1
8 - 10.5
-
pH 8.0: about 65% of maximal activity, pH 10.5: about 95% of maximal activity
8 - 11
-
pH 8.0: about 70% of maximal activity, pH 11.0: about 30% of maximal activity
8 - 11.5
-
pH 8.0: about 40% of maximal activity, pH 11.5: about 45% of maximal activity
8 - 9.5
8.5 - 10.5
-
pH 8.5: about 50% of maximal activity, about 55% of maximal activity
9 - 11
-
pH 9.0: about 35% of maximal activity, pH 11.0: about 35% of maximal activity
9.2 - 11
-
pH 9.2: about 40% of maximal activity, pH 11.0: about 60% of maximal activity
9.5 - 11.5
-
pH 9.5: about 40% of maximal activity, pH 11.5: about 45% of maximal activity, hydrolysis of beta-glycerophosphate
9.7 - 11.5
-
pH 9.7: about 60% of maximal activity, pH 11.5: about 40% of maximal activity
additional information
8 - 9.5
-
pH 8.0: about 60% of maximal activity, pH 9.5: about 75% of maximal activity
8 - 9.5
-
pH 8.0: about 90% of maximal activity, pH 9.5: about 75% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
20
25
30
35
37
40
40 - 50
45
50
56
-
native enzyme and enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
58
-
enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
60 - 70
65
80
90
40
-
native enzyme and enzymes with chemically modified aliphatic or amino groups using tetracarboxy-benzophenone derivatives
60 - 70
-
wild-type enzyme and alkaline phosphatase fused to a C-terminal region of Pseudomonas sp. MIS38 lipase
90
-
maximal activity of both free enzyme and enzyme immobilized by phosphatase-polyresorcinol complex
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
antarctic bacterium
-
10°C: about 30% of maximal activity, 40°C: about 10% of maximal activity
20 - 60
30 - 50
-
activity profile of free enzyme is comparable to immobilized enzyme
30 - 65
-
30°C: about 30% of maximal activity, 65°C: about 70% of maximal activity
30 - 70
-
the enzyme retains a high activity (more than 50%) in a wide temperature range from about 30-70°C. About 35% of its maximum phosphatase activity is retained at low (25°C) and very high (80°C) temperatures
30 - 75
-
30°C: about 60% of maximal activity of wild-type enzyme, about 45% of maximal activity of mutant enzyme os-1, 75°C: about 40% of maximal activity of wild-type enzyme, about 70% of maximal activity of mutant enzyme os-1
30 - 85
-
30°C: about 60% of maximal activity, 85°C: about 40% of maximal activity, wild-type enzyme and alkaline phosphatase fused to a C-terminal region of Pseudomonas sp. MIS38 lipase
37 - 80
25% of maximal activity at 37°C, 80% of maximal activity at 60-80°C
4 - 55
-
4°C: 43% of maximal activity, 10°C: 67% of maximal activity, 30°C: about 88% of maximal activity, 55°C: about 60% of maximal activity
45 - 60
enzyme retains a high activity between 45°C-60°C
45 - 65
-
45°C: about 60% of maximal activity, 65°C: about 40% of maximal activity
45 - 90
45°C: about 50% of maximal activity, 90°C: about 70% of maximal activity
5 - 60
-
5°C: 27% of maximal activity, 60°C: about 60% of maximal activity
50 - 95
-
50°C: about 40% of maximal activity, 95°C: about 50% of maximal activity
60 - 90
60°C: aout 50% of maximal activity, 90°C: about 40% of maximal activity
60 - 95
-
60°C: about 45% of maximal activity, 9°C: about 60% of maximal activity
65 - 85
-
65°C: about 55% of maximal activity, 85°C: about 55% maximal activity
70 - 100
Thermus sp. NTU-237
A0A1B2YKT4
at 70, 90 and 100°C, the enzyme retains more than 50% of its maximum activity at 80°C
70 - 90
-
at temperature values between 70 and 90°C, the immobilized phosphatase shows an activity about 10% higher than that of the free enzyme
20 - 60
-
20°C: about 35% of maximal activity, 60°C: about 30% of maximal activity
20 - 60
-
20°C: about 50% of maximal activity, 60°C: about 60% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
thermostable conidial and mycelial alkaline phosphatases, thermophilic fungus
-
-
brenda
Saccharomyces pombe
substrate specific enzyme form from structural gene PHO2, non specific enzyme form from structural gene PHO3 and particulate enzyme form from structural gene PHO3
-
-
brenda
2 distinct enzyme forms, an inducible enzyme form IAPase in 4 isozymes, and a constitutive enzyme form CAPase
-
-
brenda
2 distinct enzyme forms, an inducible enzyme form IAPase in 4 isozymes, and a constitutive enzyme form CAPase
-
-
brenda
-
-
-
brenda
beagle and mixed breed, 2 genes encoding 2 isozyme types: a tissue non-specific isozyme and an intestinal isozyme
-
-
brenda
gene phoA, 3 isozymes 1, 2, and 3 differing in the N-terminal sequence
-
-
brenda
gene phoA, 3 isozymes 1,2, and 3 differing in the N-terminal sequence
-
-
brenda
-
94563, 94564, 94567, 94568, 94573, 94575, 94579, 94581, 94582, 94584, 94585, 94597, 94603, 94609, 94610, 94611, 94616, 94623, 94627, 94629, 94630, 94637, 94639, 650752, 651458, 666373, 666377
-
-
brenda
-
678570, 679113, 680067, 681634, 681752, 690959, 691694, 692297, 694196, 694888, 707746, 709457, 709773, 714341, 714682
-
-
brenda
4 isozyme types: 1. nonspecific liver/bone/kidney, which is also present in osteoblast and neutrophilic granulocytes, 2. intestinal, 3. placental, 4. germ-cell
-
-
brenda
secreted alkaline phosphatase SEAP containing a single N-glycan chain, a model protein for investigation of glycosylation pattern
-
-
brenda
a major intestinal-like isoenzyme and a minor tissue-unspecific type
-
-
brenda
euryarchaeon, strain Orsay, highly thermostable enzyme
SwissProt
brenda
-
94567, 94570, 94574, 94578, 94593, 94608, 94610, 94621, 94636, 652666, 664288, 664887, 677474, 678570, 680168, 681561, 690297, 690298, 691134
-
-
brenda
substrate specific enzyme form, non specific enzyme form from structural gene PHO8, and particulate enzyme form from structural gene PHO8
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
using a monoclonal antibody against bone specific alkaline phosphatase (BAP), its expression is detected in approximately 50% of circulating B cells but not T cells. Following stimulations with Pokeweed Mitogen (PWM) and Staphylococcus aureus Cowan I (SAC), BAP expression on human B cells is increased
brenda
-
initial expression of mAPase occurs as cells progressed into S phase
brenda
-
78 160 cells from brain produce the intestinal isoenzyme
brenda
-
morphologically macrophage-like cells cloned from bone marrow cells by coculturing bone marrow cells with chondrocytes, the CCP-2 cells are similar to osteoclast but not the same
brenda
-
epididymal and seminiferous tubular epithelium, seminal plasma isozyme is of the non-specific type, secretion of the enzyme, no activity in the basal membrane of the epididymal epithelial cells
brenda
-
HeLa S3 cells from cervix produce the term-placental isoenzyme
brenda
-
three non-specific APase activities in non-permeabilized hyphal cells
brenda
-
LoVo cells from colon produce the term-placental and the intestinal isoenzyme
brenda
-
non-carcinoma tissue. Liver type alkaline phosphatesse AP is detected in the heavy and light surfactant aggregates from both non-carcinoma and squamous carcinoma tissues, but not in heavy surfactant aggregates from adenocarcinoma tissues. A larger amount of bone type alkaline phosphatase is found in light surfactant aggregate fractions from squamous cell carcinomas than those from adenocarcinoma tissues or noncarcinoma tissues from patients with either type of cancer
brenda
-
non-carcinoma tissue. Liver type alkaline phosphatesse AP is detected in the heavy and light surfactant aggregates from both non-carcinoma and squamous carcinoma tissues, but not in heavy surfactant aggregates from adenocarcinoma tissues. A larger amount of bone type alkaline phosphatase is found in light surfactant aggregate fractions from squamous cell carcinomas than those from adenocarcinoma tissues or noncarcinoma tissues from patients with either type of cancer
brenda
-
SW-620 cells from colon produce the term-placental and the liver/bone/kidney isoenzyme
brenda
-
enzyme activity of alkaline phosphatase is not observed in chondrocytes of the subperichondral and central cartilage layer of thyroid cartilage prior to cartilage mineralization. In the thyroid cartilage of a male foetus from 23rd gestational week, as well as from a 9-year-old girl and an 11-year-old boy, the enzymohistochemical reaction is negative. Beginning approximately at the middle of the second decade, the reaction product of the enzyme alkaline phosphatase is detected in distinct chondrocytes in the neighbourhood of mineralized cartilage areas or within the mineralized cartilage. In a comparison of aged-matched thyroid cartilages, male thyroid cartilage often contains more chondrocytes with a positive enzymohistochemical reaction for alkaline phosphatase than samples from females
brenda
additional information
-
matrix, articular, of proximal tibiae, highest activity in the hypertrophic zone
brenda
-
matrix, during early-stages of mineralization, in the proliferative and the hypertrophic zones
brenda
-
matrix, articular, of proximal tibiae, highest activity in the hypertrophic zone
brenda
-
associated to memebranes, and in the inter-territorial region
brenda
-
no activity in resting chondrocytes and the matrix of reserve zone
brenda
-
most efficient in presence of saturating phosphate at pH 7.1
brenda
-
most efficient in presence of saturating phosphate at pH 7.1
-
brenda
-
growing cells in the presence of increasing concentrations of MgCl2 or at increased pH values results in an almost total secretion of the enzyme to the culture filtrate
brenda
-
the enzyme is secreted during phosphate starvation
brenda
-
villous surface. HCO3- secretion increases alkaline phosphatase activity by increasing local pH at its catalytic site. Alkaline phosphatase hydrolyzes luminal phosphates, presumably ATP, which increases HCO3- secretion via activation of P2 receptors
brenda
-
neuronal and endothelial cells exclusively express the bone TNAP transcript
brenda
-
neuronal and endothelial cells exclusively express the bone TNAP transcript
brenda
-
endothelial cells exclusively express the bone TNAP transcript
brenda
-
fluid, high activity, secretion of the enzyme, localized to caput, corpora, and cauda
brenda
-
HeLa TCRC-2 cells produce the liver/bone/kidney isoenzyme, HeLa-Detroit-98 cells produce the intestinal and the liver/bone/kidney isoenzyme
brenda
-
the soluble and the membranous form are closely related but distinct isoenzymes
brenda
-
several isozymes, high activity in the upper part compared to the lower one
brenda
-
brush border of intestinal epithelial cells. Vitamin K1 and K2 as nutritional factors enhance intestinal alkaline phosphatase activity
brenda
-
enzyme activity in children after liver transplantation, overview
brenda
-
human mesenchymal stem cells produce markedly less alkaline phosphatase activity than rat mesenchymal stem cell, regardless of cell culture conditions. No difference in alkaline phosphatase activity between human MSCs grown on 45S5 bioactive glass or tissue culture plastic, in samples from five different orthopaedic patients, regardless of culture media composition
brenda
-
elevated levels of alkaline phosphatase activity when grown on 45S5 bioactive glass as compared to standard tissue culture plastic. Similarly, exposure to the dissolution products of 45S5 elevates alkaline phosphatase activity and other osteogenic markers in these cells
brenda
-
chela muscle. Levamisole-insensitive alkaline phosphatase activity
brenda
-
chela muscle, levamisole-sensitive alkaline phosphatase activity
brenda
-
neuronal and endothelial cells exclusively express the bone TNAP transcript
brenda
-
neuronal and endothelial cells exclusively express the bone TNAP transcript
brenda
-
neuronal cells express the bone as well as the liver TNAP transcript
brenda
the placental isoenzyme is encoded by a gene identical to the gene expressed in mouse, liver, kidney, and tetracarcinoma stem cells
brenda
-
osteosarcoma cells, contain isozymes of the bone alkaline phosphatase form, main isozymes are B1 and B2, and intestinal alkaline phosphatase form, e.g. isozyme B/I which is composed of 70% bone and 30% intestinal enzyme
brenda
-
seminal plasma specific isozyme of the non-specific type
brenda
-
transient elevation of enzyme activity after liver transplantation in children showing specific isoenzyme pattern of benign transient hyperphosphatasemia
brenda
-
contains isozymes of the bone alkaline phosphatase form, main isozymes are B1 and B2, and intestinal alkaline phosphatase form, e.g. isozyme B/I which is composed of 70% bone and 30% intestinal enzyme
brenda
-
low activity, localized on the surface of the seminiferous epithelial cells and tubules
brenda
-
restricted mesenchymal and epithelial regions. Its localization and strength changes during the hair cycle. Activity in the dermal papilla is moderate in very early anagen, reaches a maximal level in early anagen, decreases at the proximal region of dermal papilla after mid anagen, and is kept at a low level during catagen. The bulbar dermal sheath shows intense alkaline phosphatase activity only in early anagen. Most bulbar epithelium does not show alkaline phosphatase activity, germinative epidermal cells that are adjacent to the alkaline phosphatase-negative dermal papilla cells become alkaline phosphatase-positive in mid anagen and rearrange in a single layer so as to encapsulate the dermal papilla in mid catagen. During catagen, the outermost layer of bulbar epithelium becomes alkaline phosphatase-positive, which could be follicular epithelial precursors migrating from the bulge. Before the initiation of hair formation, alkaline phosphatase activity in the bulbar epithelium rapidly decreases and that in dermal papilla increases. These dynamic changes of alkaline phosphatase expression might be related to functions of the dermal papilla in hair induction and also to reconstruction of the bulbar structure during the hair cycle
brenda
-
restricted mesenchymal and epithelial regions. Its localization and strength changes during the hair cycle. Activity in the dermal papilla is moderate in very early anagen, reaches a maximal level in early anagen, decreases at the proximal region of dermal papilla after mid anagen, and is kept at a low level during catagen. The bulbar dermal sheath shows intense alkaline phosphatase activity only in early anagen. Most bulbar epithelium does not show alkaline phosphatase activity, germinative epidermal cells that are adjacent to the alkaline phosphatase-negative dermal papilla cells become alkaline phosphatase-positive in mid anagen and rearrange in a single layer so as to encapsulate the dermal papilla in mid catagen. During catagen, the outermost layer of bulbar epithelium becomes alkaline phosphatase-positive, which could be follicular epithelial precursors migrating from the bulge. Before the initiation of hair formation, alkaline phosphatase activity in the bulbar epithelium rapidly decreases and that in dermal papilla increases. These dynamic changes of alkaline phosphatase expression might be related to functions of the dermal papilla in hair induction and also to reconstruction of the bulbar structure during the hair cycle
-
brenda
-
both 20-hydroxyecdysone feeding of the flies and juvenile hormone application leads to a substantial rise in ALP activity. ALP activity in young females of a juvenile hormone-deficient strain of Drosophila melanogaster, apterous56f is lower than activity in wild type
brenda
-
both 20-hydroxyecdysone feeding of the flies and juvenile hormone application leads to a substantial rise in ALP activity
brenda
additional information
-
tissue distribution, 2 isozyme types: a tissue non-specific isozyme and an intestinal isozyme type, different forms of these isozymes are bone, liver, seminal plasma and kidney enzymes of the non-specific type, and intestine and corticosteroid-inducible enzymes of the intestinal type
brenda
additional information
-
located at the secondary ossification site of hamster humerus
brenda
additional information
-
no or poor activity in spermatozoa and pre-ejaculatory fluid, respectively
brenda
additional information
-
4 isozyme types: 1. nonspecific liver/bone/kidney, which is also present in osteoblast and neutrophilic granulocytes, 2. intestinal, 3. placental, 4. germ-cell
brenda
additional information
-
the different enzyme forms differ in their half-lives of circulation
brenda
additional information
-
in biofilms and colonies alkaline phosphatase is initially expressed in the region of the biofilm immediately adjacent to the carbon and energy source (glucose). In time, the region of alkaline phosphatase expression expanded inward until it spanned most, but not all, of the biofolm or colony depth. Alkaline phosphatase expression patterns are primarily controlled by the local availability of either the carbon and energy source or the electron acceptor
brenda
additional information
-
in biofilms and colonies alkaline phosphatase is initially expressed in the region of the biofilm immediately adjacent to the carbon and energy source (glucose). In time, the region of alkaline phosphatase expression expanded inward until it spanned most, but not all, of the biofolm or colony depth. Alkaline phosphatase expression patterns are primarily controlled by the local availability of either the carbon and energy source or the electron acceptor
-
brenda
additional information
no TNALP reactivity is found in the osteocyte
brenda
additional information
-
expression of alkaline phosphatase in biofilms occurs in a thin, sharply delineated band at the biofilm-bulk fluid interface. Alkaline phosphatase expression patterns are primarily controlled by the local availability of either the carbon and energy source or the electron acceptor
brenda
additional information
SmAP gene is most highly expressed in intravascular parasite life stages. Using immunofluorescence and immuno-electron microscopy, it is shown that SmAP is expressed at the host/parasite interface and in internal tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ALP is localized in the Golgi area of the cytoplasm in solitary McA-RH 7777 cells cultured at low concentration. Contact between McA-RH 7777 cells promotes the translocation of ALP from the Golgi area of the cytoplasm to the plasma membrane. Colchicine caused siruption of the Golgi complex into fragments, which scatters throughout the cytoplasm, does not interfere with translocation of ALP to the plasma membrane
brenda
-
hepatocytes cultured in colchicine-containing medium
brenda
additional information
-
the enzyme is located either in the periplasmic space or is loosely bound to the cells wall
brenda
Synechococcus elongatus PCC 7942 = FACHB-805 R2
-
the enzyme is located either in the periplasmic space or is loosely bound to the cells wall
-
brenda
-
interstitial space, associated with the subjacent apical plasma membrane of the syncytiotrophoblast
-
brenda
-
the enzyme is secreted during phosphate starvation
-
brenda
-
BALP is an ectoenzyme attached to the osteoblast cell membrane by a glycosylphosphatidylinositol anchor
-
brenda
-
membrane-bound exoenzyme which faces the extracellular compartment
brenda
-
decidual cell membrane, apical plasma membrane of the syncytiotrophoblast
brenda
-
the enzyme is secreted during phosphate starvation
brenda
-
bone isoenzyme is oriented towards the outside of the plasma membrane in linkage to phosphatidylinositol
brenda
-
covalent attachment of the hydrophobic phosphatidylinositol membrane anchor causes the amphiphilic form to behave anomalously on electrophoresis
brenda
-
BALP is an ectoenzyme attached to the osteoblast cell membrane by a glycosylphosphatidylinositol anchor
brenda
-
associated to the outside of cell membranes of chondrocytes
brenda
TNALP is intensely localized on the basolateral cell membranes of mature osteoblasts and preosteoblastic cells
brenda
ALP is found in the soluble form as well as in the insoluble form bound to the mebrane via a GPI anchor
brenda
-
in hepatocytes cultured in basal medium, ALP is localized in the perinuclear cytoplasm
-
brenda
-
released from the periplasmic space into the culture supernatant as a soluble form
-
brenda
-
released from the periplasmic space into the culture supernatant as a soluble form
-
-
brenda
-
the enzyme is located either in the periplasmic space or is loosely bound to the cells wall
-
brenda
Synechococcus elongatus PCC 7942 = FACHB-805 R2
-
the enzyme is located either in the periplasmic space or is loosely bound to the cells wall
-
-
brenda
-
enzyme is closely associated with the inner region of the tripartite layer and is never observed to be associated with the cytoplasmic membrane
brenda
-
when hepatocytes are cultured in dexamethasone-supplemented medium, ALP is also localized in the plasma membrane surrounding the bile canaliculus-like structure that is formed between adjacent cells
brenda
-
hepatocytes cultured in dexamethason-supplemented medium
brenda
-
the enzyme from intestine is mainly a soluble constituent of the mucosal cells
-
brenda
ALP is found in the soluble form as well as in the insoluble form bound to the mebrane via a GPI anchor
-
brenda
additional information
-
in Alexandrium catenella alkaline phosphatase covers the whole cell, and the alkaline phosphatase production sites are mainly in the cell with only some on the cell surface
-
brenda
additional information
-
temperature-dependent localization of the glycosylphosphatidylinositol-anchored bovine intestinal alkaline phophatase into model raft made of palmitoyloleoylphosphatidylcholine/sphingomyelin/cholesterol supported membranes. Atomic force microscopy shows that the inserted BIAP is localized in the sphingomyelin/cholesterol enriched ordered domains at low temperature. Above 30°C, BIAP redistributes and is present in both the fluid palmitoyloleoylphosphatidylcholine enriched and the ordered sphingomyelin/cholesterol domains
-
brenda
additional information
-
the enzyme from liver is associated with the particulate fractions such as nuclei, mitochondria and lysosomes
-
brenda
additional information
-
in Prorocentrum donghaiense, alkaline phosphatase covers most of the cell, and the alkaline phosphatase production sites are mainly on the cell surface, although some can be observed inside cells
-
brenda
additional information
-
in hepatocytes cultured in the same medium containing colchicine, the structure of microtubules in the cytoplasm is lost, ALP is localized in coarse granular sites of the cytoplasm
-
brenda
additional information
-
in Skeletonema costatum only one or two alkaline phosphatase production sites can be detected, which are all on the cell surface
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
detailed computational structural and functional characterization and phylogenetic studies of alkaline phosphatase from nine different strains of Rhizobium leguminosarum, including active site prediction and functional motif prediction. Seven out of nine strains are closely related and other two were distantly related
malfunction
metabolism
physiological function
malfunction
the ability of living parasites to cleave exogenous adenosine monophosphate and generate adenosine is very largely abolished when SmAP gene expression is suppressed following RNAi treatment targeting the gene
malfunction
deletion of OE5192R produces a mutant strain with virtually no phosphatase activity
malfunction
-
enzyme deficiency diminishes chondrocyte vascular endothelial cell growth factor expression
malfunction
mutations L37P, Y178H (i.e. c.110T>C, c.532T>C) and D239Y (i.e. c.715G>T) are identified in two children with extreme hypophosphatasia phenotype. Mutants 1 and 2 demonstrate negligible alkaline phosphatase activity and mineralization is 7.9% and 9.3% of wild-type, respectively. Mutant 3 demonstrates about 50% alkaline phosphatase activity and 15.5% mineralization of wild-type
metabolism
two chloride binding sites are present in the structure, one in the active site and another one at a peripheral site. Upon binding of chloride to the peripheral site, structural dynamics decrease locally, resulting in thermal stabilization of the VAP active conformation. Binding of the chloride ion in the active site does not displace the bound inorganic phosphate product, but it may promote product release by facilitating rotational stabilization of the substrate-binding Arg129
metabolism
-
residue Ser 94 acts as nucleophil and is activated by the Zn ion. Arg 145 is mobile due to its location in the loop region, and stabilizes the substrate through direction or water-mediated secondary interaction. The putative residues mainly involved in the catalysis are Ser 94, Ser 141, Ala 146, Thr 147, Pro 148, Asp 293, and Glu 294
metabolism
calf intestinal alkaline phosphaase has only minimal activity against unmodified enteric lipopolysaccharide chemotypes. Phosphate is only released from a subset of lipopolysaccharide chemotypes harboring spontaneously labile phosphoethanolamine modifications connected through phosphoanhydride bonds
physiological function
-
Daphnia magna eating phosphorus-poor food have significantly higher alkaline phosphatase activity in their bodies compared with individuals eating phosphorus-rich food. By contrast, poor phosphorus-nutrition of Daphnia lowers alkaline phosphatase activity in released materials compared with that measured from their phosphorus-sufficient conspecifics
physiological function
-
in neonatal blood plasma, soluble 5'-nucleotidase and alkaline phosphatase mediate conversion of AMP to adenosine, whereas soluble adenosine deaminase catabolizes adenosine to inosine. Newborn blood plasma demonstrates substantially higher adenosine-generating 5'-nucleotidase and alkaline phosphatase activity and lower metabolizing adenosine deaminase activity than adult plasma. Abundant alkaline phosphatase expressed on the surface of circulating neonatal neutrophils is the dominant AMPase on these cells
physiological function
-
the enzyme plays an important role in biofilm formation
physiological function
Daphnia commutata
-
the enzyme is a phosphorus deficiency indicator in zooplankton
physiological function
-
the enzyme influences chondrocyte maturation, apoptosis, and MAPK signaling in a cell autonomous manner. The enzyme is essential for the later stages of endochondral bone development including hypertrophic chondrocyte apoptosis and vascular endothelial cell growth factor-mediated recruitment of blood vessels for replacement of cartilage with bone
physiological function
-
the Aedes aegypti enzyme is involved in the toxicity of Cry toxins from Bacillus thuringiensis subsp. israelensis and jegathesan. The enzyme is an important secondary receptor for Cry11Aa and Cry11Ba, but not involved in Cry4Aa and Cry4Ba toxicity
physiological function
the enzyme is crucial for bone matrix mineralization
physiological function
-
there is no significant relation between enzyme activity and calcium and phosphate concentrations in saliva
physiological function
TNALP facilitates mineralization by providing phosphate and is found relatively distant from the osteoid, while ectonucleotide diphosphatase/phosphodiesterase ENPP1, which inhibits mineralization by providing diphosphates, is localized in close proximity of the osteoid
physiological function
in transgenic rice overexpressing phoA, phosphate loss is minimized and overexpression contributes to weed management in the agriculture. The phoA rice lines show improved root, shoot length and total biomass production under phosphite conditions. The phenotype and productivity of phoA lines under the phosphite treatment attain are similar to that of plants under phosphate sufficient condition
physiological function
-
alkaline phosphatase interacts with Cry1Ac toxin in vitro. In vitro incubation of Cry1Ac toxin with the purified alkaline phosphatase results in a 43% decrease in alkaline phosphatase specific activity. When Cry1Ac toxin is supplied to the diet of caterpillars, it is efficient in decreasing larval weight gain and survival
physiological function
-
the enzyme plays an important role in biofilm formation
-
Show AA Sequence and Transmembrane Helices (11175 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
105000
108000
110000
120000
130000
136000
138000
150000
160000
200000
220000
-
hydrophilic enzyme from osteosarcoma cells, density gradient gel electrophoresis
227000
-
hydrophilic enzyme from lymphoma cells L248, density gradient gel electrophoresis
40000
44000
recombinant mutant T59R, sucrose density gradient sedimentation
45000
47000
483000
-
amphiphilic enzyme from osteosarcoma cells, density gradient gel electrophoresis
494000
-
amphiphilic enzyme from lymphoma cells L248, density gradient gel electrophoresis
50000
52000
54000
55000
56000
57000
58000
58500
-
2 * 58500, mycelial enzyme fomr, SDS-PAGE, 2 * 63000, conidial enzyme form, SDS-PAGE
59000
60000
62000
63000
-
2 * 58500, mycelial enzyme fomr, SDS-PAGE, 2 * 63000, conidial enzyme form, SDS-PAGE
64000
65000
66000
68000
70000
72000
75000
76000
80000
81000
87000
additional information
110000
mass spectrometric analysis of SDS-PAGE-separated protein
160000
-
x * 160000, SDS-PAGE, the native form of the enzyme is heterogeneous and composed of multiple oligomeric forms
45000
-
8 * 45000, sucrose-density gradient sedimentation, quarternary structure, conformation of the majority of the enzyme
50000
mass spectrometric analysis of SDS-PAGE-separated protein
59000
x * 59000 (predicted), 68000 (estimated), Western Blot analysis
62000
-
x * 62000 or x * 65000, the purified recombinant enzyme appears in two subunit sizes, 62000 Da and 65000 Da, due to heterogenous N-glycosylation, SDS-PAGE
64000
-
1 * 64000, recombinant enzyme, SDS-PAGE, 1 * 66200, native enzyme, SDS-PAGE
65000
-
x * 62000 or x * 65000, the purified recombinant enzyme appears in two subunit sizes, 62000 Da and 65000 Da, due to heterogenous N-glycosylation, SDS-PAGE
66000
-
immunoblotting, immature form bearing high mannose-type N-linked oligosaccharides
68000
-
4 * 68000, the enzyme also exists in a dimeric form, SDS-PAGE after treatment with 2-mercaptoethanol
87000
recombinant wild-type and mutant T59A enzymes, sucrose density gradient sedimentation
additional information
-
the enzyme appears as a broad peak at a location corresponding to molecules having molecular masses of 650 to 850 kDa. The native form of the enzyme is heterogeneous and composed of multiple oligomeric forms
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
octamer
-
8 * 45000, sucrose-density gradient sedimentation, quarternary structure, conformation of the majority of the enzyme
tetramer
additional information
?
-
x * 160000, SDS-PAGE, the native form of the enzyme is heterogeneous and composed of multiple oligomeric forms
?
x * 59000 (predicted), 68000 (estimated), Western Blot analysis
?
-
x * 62000 or x * 65000, the purified recombinant enzyme appears in two subunit sizes, 62000 Da and 65000 Da, due to heterogenous N-glycosylation, SDS-PAGE
dimer
-
activity of the dimer is three or four times higher than that of the tetramer
dimer
-
activity of the dimer is three or four times higher than that of the tetramer
dimer
activity of the dimer is three or four times higher than that of the tetramer
dimer
enzyme forms dimers composed of dominant beta-sheet structures sandwiched by alpha-helices. Active sites are well-accessible
dimer
-
2 * 58500, mycelial enzyme fomr, SDS-PAGE, 2 * 63000, conidial enzyme form, SDS-PAGE
dimer
-
the 90000 Da monomeric species dimerises to about 180000 Da upon purification
homodimer
-
sucrose density gradient centrifugation, wild-type and V406A form a homodimer
monomer
antarctic bacterium HK47
-
1 * 68000, SDS-PAGE after treatment with 2-mercaptoethanol
-
monomer
-
1 * 64000, recombinant enzyme, SDS-PAGE, 1 * 66200, native enzyme, SDS-PAGE
tetramer
-
4 * 68000, the enzyme also exists in a dimeric form, SDS-PAGE after treatment with 2-mercaptoethanol
additional information
-
heterodimer formation in vitro, overview, structural assembly of the enzyme into dimer induces cooperative interactions between the monomers necessary for the formation of the functional form of the holoenzyme
additional information
Thr59 is involved in stabilization of the dimeric interface, structural analysis
additional information
-
Thr59 is involved in stabilization of the dimeric interface, structural analysis
additional information
both monomeric and dimeric enzyme forms exist, no cysteine residues are involved in intramolecular disulfide bonds
additional information
-
both monomeric and dimeric enzyme forms exist, no cysteine residues are involved in intramolecular disulfide bonds
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
side-chain modification
glycoprotein
-
sialic acid containing carbohydrates, different pattern for the different isozymes
glycoprotein
-
N-linked oligosaccharides containing terminal N-acetylgalactosamine
glycoprotein
-
N-glycosylated, isozymes B1, B2, and B/I, contain different amounts of carbohydrates with terminal sialic acids, total carbohydrate content of the isozymes is 14% for B/I, 21% for B1, and 23% for B2
glycoprotein
-
secreted alkaline phosphatase SEAP containing a single N-glycan chain, a model protein for investigation of glycosylation patterns, recombinant enzymes expressed in insect cells shows differing patterns: Sf-9 cell derived enzyme has Mna4GlcNAc2 and FucMan4GlcAc2 as major N-glycans, while the Tn-5B1-4 cell derived enzyme has Man2GlcAc2 as major N-glycan, glycan structures overview
glycoprotein
mature form of 80 ka bears complex-type oligosaccharides. The 80 kDa form is sensitive to neuraminidase, but is resistant to treatment with Endo H
glycoprotein
-
carbohydrate content of mycelial enzyme form is 63% and of conidial enzyme form is 54%
side-chain modification
-
two N-linked and one or more O-linked glycoconjugates per monomer: isoenzymes C1, C2 and B2 have similar sugar types but C2 contains significantly more carbohydrate than the adult enzyme. Galactose, mannose, N-acetylglucosamine and lesser amounts of N-acetylgalactosamine, sialic acid and fucose
side-chain modification
-
in vitro glycosylation of the enzyme and consecutive alteration of its activity and structure
side-chain modification
-
calf intestinal enzyme contains about 20% hexose + hexosamine
side-chain modification
-
the purified recombinant enzyme appears in two subunit sizes, 62000 Da and 65000 Da, due to heterogenous N-glycosylation. There are two putative N-glycosylation sites in the primary sequence, Asn122-Thr-Thr and Asn249-Arg-Thr, only the latter appears to be glycosylated in the naive enzyme
side-chain modification
disparities in the molecular mass of the mouse enzyme from placenta, 86000 Da, liver, 76000 Da, and kidney, 79000 Da, are probably due to differences in glycosylation
side-chain modification
-
glycoprotein, the soluble form contains more fucose and N-acetylgalactosamine than does the membranous form. The soluble enzyme form contains 19.8% carbohydrate, the membranous enzyme form contains 16% carbohydrate
side-chain modification
-
glycoprotein, contains at least 20% by weight of carbohydrate
side-chain modification
-
glycoprotein is anchored to the membrane by the glycosyl-phosphatidylinositol linkage
side-chain modification
-
the non-speficic enzyme form is a glycoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 2.1 A X-ray diffraction structure of Arg166Ser alkaline phosphatase is presented, which shows little difference in enzyme structure compared to the wild-type enzyme but shows a significant reorientation of the bound phosphate
crystal structure of the covalent phospho-enzyme intermediate of the H331Q mutant enzyme and of the transition state complex between the wild-type enzyme and vanadate
hanging drop vapour diffusion method, structures if the inactive wild-type enzyme with cobalt anf the structure of the active D153H/K328W enzyme with cobalt
mutant enzyme D101A/D153A, hanging drop vapor diffusion method, using 22% (w/v) PEG3350, 0.1 mM Bis-Tris, pH 5.0, 0.2 mM ammonium sulfate
diffracting crystals are grown using the hanging-drop vapor diffusion method. Crystallographic data are collected to a resolution of 1.7 A
to 2.1 A resolution. The unit cell contains one dimer unit corresponding to the biological unit. The surface of the dimer is substantially more acidic than that of the Vibrio sp. G15-21 alkaline phosphatase dimer, and may enable the solubility of Halomonas sp. alkaline phosphatase under high-salt conditions. The monomer unit of Halomonas sp. alkaline phosphatase forms a substantially larger hydrophobic interior comprising 329 C atoms from completely buried residues compared with Vibrio sp. G15-21 alkaline phosphatase
10-16 mg/ml purified enzyme in 10 mM Tris, pH 7.0, 2 mM MgCl2, 0.02% NaN3, sitting drop vapour diffusion method, free or in complex with substrate 4-nitrophenyl phosphate, reservoir solution: 12-14% PEG 4000, 20% PEG 3350, 2 mM zinc acetate, 100 mM sodium cacodylate, pH 6.5, the buffer can also be acetate, citrate or imidazole malate, X-ray diffraction structure determination and analysis at 1.9 A resolution
homology modeling and molecular docking of substrate. The complex with 4-nitrophenyl phosphate has a binding energy of -5.9 kcal/mol
-
11 mg/ml purified protein, in presence 0.1 mM Zn2+ and 1.0 mM Mg2+, hanging drop vapour diffusion method, crystallization buffer: 42.5% w/v ammoniums sulfate, 10% v/v glycero, 100 mM Tris-maleate, pH 5.6, X-ray diffraction structure determination and analysis at 1.9 A resolution, structure modeling
shrimp
-
10 mg/ml, purified recombinant enzyme, hanging-drop vapour-diffusion method, equal volumes of protein and precipitant solution, precipitant solution: 140 mM MgCl2, 100 mM HEPES, pH 7.5, 28.5% PEG 400, X-ray diffraction sturcture determinationand analysis at 2.16 A
-
crystal structure of the enzyme at 1.4 A resolution is reported and compared to alkaline phosphatases from other species. The surface does not have the high negative charge density as observed in shrimp alkaline phosphatase, but a positively charged patch is observed around the active site that may be favourable for substrate binding. The dimer interface has a similar number of non-covalent interactions and the crown-domain is the largest observed in known alkaline phosphatases. The catalytic serines are refined with multiple conformations in both monomers. One of the ligands to the catalytic zinc ion in binding site M1 is directly connected to the crown-domain and is closest to the dimmer interface. Subtle movements in metal ligands may help in the release of the product and/or facilitate prior dephosphorylation of the covalent intermediate
-
crystallization in presence of NaCl, bromide and HEPES. Two chloride binding sites are found in the structure, one in the active site and another one at a peripheral site
to 2.3 A resolution. Cyclohexyamine is found at two binding sites, one in the active site channel and another at the surface close to dimer interface
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D460A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
D505A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
E445A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
H216A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
H464A
-
mutant is almost inactive in 1 M Tris buffer, but has an increased activity in 0.1 M Mops buffer
H506A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
H566A
-
mutant is almost inactive in 1 M Tris buffer, but has an increased activity in 0.1 M Mops buffer
R229A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
S165A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
T218A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
G149D
mutant shows increased activity after thermal inactivation at 60°C, 120 min: 11.4%, kcat (1/sec) (4-nitrophenyl phosphate): 117
G87A
mutant shows increased activity after thermal inactivation at 60°C, 120 min: 11.4%, kcat (1/sec) (4-nitrophenyl phosphate): 100
H135E
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 0.4%, kcat (1/sec) (4-nitrophenyl phosphate): 303
H135E/G149D
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 1%, kcat (1/sec) (4-nitrophenyl phosphate): 361
S338T
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 0.6%, kcat (1/sec) (4-nitrophenyl phosphate): 114
S42G
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 0%, kcat (1/sec) (4-nitrophenyl phosphate): 133
S42G/H135E
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 0%, kcat (1/sec) (4-nitrophenyl phosphate): 70
S42G/S338T
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 0%, kcat (1/sec) (4-nitrophenyl phosphate): 71
S86A
mutant shows increased activity after thermal inactivation at 60°C, 120 min: 15.6%, kcat (1/sec) (4-nitrophenyl phosphate): 203
S86A/G87A
double mutant shows increased activity after thermal inactivation at 60°C, 120 min: 39.4%, kcat (1/sec) (4-nitrophenyl phosphate): 30
biotechnology
aqueous suspendible polymer nanostructures are prepared by simple microtome processing of electrospun nylon 6 nanofibers and are used to immobilize calf intestinal ALP by either covalent or noncovalent bioconjugation chemistries. Noncovalent immobilization of ALP to the mechanically cut nanofibers using a multi-stacked, layer-by-layer approach with the cationic polymer Sapphire II results in the highest enzyme loading. In terms of the overall catalytic performance of the various immobilized ALP systems, a single-stacked layer-by-layer assembly approach resulted in the highest level of enzymatic activity (30.1%) per unit mass of nanofiber support
G168K
-
kcat value 2times that of the wild-type with substrate 6,8-difluoro-4-methylumbelliferyl phosphate, and kcat similar to that of the wild-type with substrate methylumbelliferyl phosphate
G168R
-
kcat value 2times that of the wild-type with substrate 6,8-difluoro-4-methylumbelliferyl phosphate, and kcat similar to that of the wild-type with substrate methylumbelliferyl phosphate
D101A
the mutant shows 64fold decreased catalytic efficiency compared to the wild type enzyme
D101A/D153A
the mutant shows 190fold decreased catalytic efficiency compared to the wild type enzyme
D101A/D153A/E322Y
the mutant shows 48000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/D153A/E322Y/K328A
the mutant shows 320000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/D153A/K328A
the mutant shows 5300fold decreased catalytic efficiency compared to the wild type enzyme
D101A/E322Y
the mutant shows 20000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/E322Y/K328A
the mutant shows 570000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/K328A
the mutant shows 23000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S
the mutant shows 11000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/D153A
the mutant shows 32000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/D153A/E322Y
the mutant shows 670000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/D153A/E322Y/K328A
the mutant shows 3700000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/D153A/K328A
the mutant shows 120000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/E322Y
the mutant shows 15000000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/E322Y/K328A
the mutant shows more than 30000000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/K328A
the mutant shows 2300000fold decreased catalytic efficiency compared to the wild type enzyme
D101S
D153A
the mutant shows 230fold decreased catalytic efficiency compared to the wild type enzyme
D153A/E322Y
the mutant shows 270000fold decreased catalytic efficiency compared to the wild type enzyme
D153A/E322Y/K328A
the mutant shows 2000000fold decreased catalytic efficiency compared to the wild type enzyme
D153A/K328A
the mutant shows 1400fold decreased catalytic efficiency compared to the wild type enzyme
D153G
D153H
reduced magnesium affinity, maximual activity is only achieved with the addition of exogenous magnesium
D153H/K328A
reduced magnesium affinity, maximal activity is only achieved with the addition of exogenous magnesium
D153H/K328W
mutant enzyme containing Co2+ has higher catalytic efficiency than the wild-type enzyme containing cobalt
D369N
D434E
-
site-directed mutagenesis, reduced activity, increased kcat and Km compared to the wild-type enzyme
E22Y
kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 7200, (3-nitrobenzyl phosphate): 31, (methyl phosphate): 1.6, (methyl 4-nitrophenyl phosphate): 35, (bis-4-nitrophenyl phosphate): 0.07, (4-nitrophenyl sulfate): 0.0000029
E322Y/K328A
the mutant shows 420000fold decreased catalytic efficiency compared to the wild type enzyme
E332Y
the mutant shows 88000fold decreased catalytic efficiency compared to the wild type enzyme
K328A
R166A
R166Q
mutation has very little effect on turnover number, in presence of phosphate acceptor the substrate binding decreases over 50fold
R166S
R166S/D153A
the mutant shows 49000fold decreased catalytic efficiency compared to the wild type enzyme
R166S/D153A/E322Y
the mutant shows 33000000fold decreased catalytic efficiency compared to the wild type enzyme
R166S/D153A/E322Y/K328A
the mutant shows 140000000fold decreased catalytic efficiency compared to the wild type enzyme
R166S/D153A/K328A
the mutant shows 180000fold decreased catalytic efficiency compared to the wild type enzyme
R166S/E322Y
R166S/E322Y/K328A
the mutant shows 1600000000fold decreased catalytic efficiency compared to the wild type enzyme
R166S/K328A
the mutant shows 2600000fold decreased catalytic efficiency compared to the wild type enzyme
S102A
activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction,1000-10000fold reduction in the turnover number
S102C
activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction, 100fold reduction in turnover number
S102G
activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction, 1000-10000fold reduction in the turnover number
S102L
activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction, 1000-10000fold reduction in the turnover number
T59A
site-directed mutagenesis, exists as a dimer, shows catalytic activity and metal content similar to the wild-type enzyme
T59R
site-directed mutagenesis, exists as a monomer, shows 10000fold reduced activity compared to the wild-type, highly reduced metal content, highly reduced thermal stability
T81A
-
the T81A mutant displays a somewhat lower affinity than the wild-type enzyme for both substrate and phosphate, while kcat does not change significantly
W109I
-
kcat value 5 to 8 times that of the wild-type with substrate 6,8-difluoro-4-methylumbelliferyl phosphate, and kcat value 9 to 17 times that of the wild-type with substrate methylumbelliferyl phosphate
W109L
-
kcat value 5 to 8 times that of the wild-type with substrate 6,8-difluoro-4-methylumbelliferyl phosphate, and kcat value 9 to 17 times that of the wild-type with substrate methylumbelliferyl phosphate
W322A
kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 8900, (3-nitrobenzyl phosphate): not determined, (methyl phosphate): not determined, (methyl 4-nitrophenyl phosphate): 18, (bis-4-nitrophenyl phosphate): 0.037, (4-nitrophenyl sulfate): not determined
A116T
-
mutant responsible for hypophosphatasia shows negligible alkaline phosphatase activity and a weak dominant negative effect when co-expressed with the wild-type enzyme, mutant exists as a monomer and heterogeneously associated aggregates covalently linked via disulfide bonds in contrast to wild-type enzyme which exists as a homodimer
A16V
-
in combination with P275T the mutation causes infantile hypophosphatasia, 7.2% of wild-type activity
C201Y
mutation identified in patient diagnosed with perinatal hypophosphatasia. Mutants exhibit a diminished alkaline phosphatase activity in the cells, where a 66 kDa immature form is predominant with a marginal amount of a 80 kDa mature form. The 66 kDa form exists as a monomer in contrast to a dimer form of wild-type. Only a small fraction of the mutant protein reaches cell surface as the 80 kDa mature form, most of the 66 kDa form is found to be endo-beta-N-acetylglucosaminidase H sensitive and rapidly degraded in proteasome following polyubiquitination
C489S
mutation identified in patient diagnosed with perinatal hypophosphatasia. Mutants exhibit a diminished alkaline phosphatase activity in the cells, where a 66 kDa immature form is predominant with a marginal amount of a 80 kDa mature form
D239Y
i.e. c.715G>T, mutant identified in a child with extreme hypophosphatasia phenotype. Mutant demonstrates about 50% alkaline phosphatase activity and 15.5% mineralization of wild-type
G420A
naturally occuring mutant, reported in perinatal and childhood hypophosphatasia. Mutant lacks its alkaline phosphatase activity
G420S
naturally occuring mutant, reported in perinatal and childhood hypophosphatasia. Mutant lacks its alkaline phosphatase activity, although mutant protein is anchored to the cell surface lipid bilayers by glycosylphosphatidylinositol as an 80 kDa mature form bearing complex-type oligosaccharides similar to wild-type. Mutant G420S largely fails to assemble into the homodimer in contrast to wild-type
L37P
i.e. c.110T>C, mutation identified in a child with extreme hypophosphatasia phenotype. Mutant demonstrates negligible alkaline phosphatase activity and mineralization is 7.9% of wild-type
N417D
mutation abolishes the dimerization without perturbing its cell surface localization
N417E
mutation abolishes the dimerization without perturbing its cell surface localization
N417S
mutation associated with severe hypophosphatasia, mutants lack enzymic activity. Mutant undergoes N-linked oligosaccharide processing and appears on the cell surface similar to wild-type. Mutant fails to assemble into a dimer structure, which is needed for the catalytic function
P108L
inactive, the mutation is associated with dominant odontohypophosphatasia
P275T
-
in combination with A16V mutation causes infantile hypophosphatasia, 4% of wild-type activity
R119H
-
in combination with Y280D the mutation causes childhood hypophosphatasia, 33.4% of wild-type activity
R166A
-
mutation changes the inhibition mechanism of the mutant enzyme to a more complex mixed-type inhibition with decreased affinities for L-Leu and L-Phe
R255H
-
mutation (homozygote) causes infantile hypophosphatasia, 6.8% of wild-type activity
V406A
-
mutant protein shows a markedly reduced alkaline phosphatase activity. Mutant is conveyed to the Golgi apparatus and incorporated into a cold detergent insoluble fraction (raft) at a rate similar to that of the wild-type. Mutant shows increased susceptibility to digestion by trypsin or proteinase K. When purified as a glycosylphosphatidylinositol-anchorless soluble form, mutant protein exhibits a remarkably lower Kcat /Km value compared with that of the wild-type TNSALP
V406F
-
replacement with phenylalanine results in a low enzyme activity, even though TNSALP (V406F) is processed to the 80 kDa mature form similarly to TNSALP (V406A) and appears on the cell surface like the wild-type protein
V406I
-
similar to wild-type, leucine and isoleucine can be successfully substituted for the valine residue
V406L
-
similar to wild-type, leucine and isoleucine can be successfully substituted for the valine residue
Y178H
i.e. c.532T>C, mutant identified in a child with extreme hypophosphatasia phenotype. Mutant demonstrates negligible alkaline phosphatase activity and mineralization is 9.3% of wild-type
Y280D
-
in combination with R119H the mutation causes childhood hypophosphatasia, 1.3% of wild-type activity
K161S/K184S
the mutant shows much higher residual specific activity after maleimide activation than the wild type enzyme
K171A
residual specific activity is three orders of magnitude lower than that of the wild-type
R173A
residual specific activity is three orders of magnitude lower than that of the wild-type
T89S
residual specific activity is three orders of magnitude lower than that of the wild-type
G51C
-
kcat for 4-nitrophenyl phosphate is 15.8fold lower than wild-type enzyme. Km-value for 4-nitrophenyl phosphate is 2.8fold lower than wild-type value
H116D
-
slightly less heat-stable than the wild-type enzyme. Mutant enzyme shows much reduced catalytic efficiencies as compared to the wild-type enzyme. kcat/KM is 29.7fold lower than wild-type value
H116D/W274K
-
more heat-tolerant than the wild-type enzyme. Mutant enzyme shows much reduced catalytic efficiencies as compared to the wild-type enzyme. kcat/KM is 17.1fold lower than wild-type value
I50C
-
kcat for 4-nitrophenyl phosphate is 6fold lower than wild-type enzyme. Km-value for 4-nitrophenyl phosphate is 2.4fold lower than wild-type value
S52C
-
kcat for 4-nitrophenyl phosphate is 10.2fold lower than wild-type enzyme. Km-value for 4-nitrophenyl phosphate is 1.9fold lower than wild-type value
S53C
-
kcat for 4-nitrophenyl phosphate is 9.6fold lower than wild-type enzyme. Km-value for 4-nitrophenyl phosphate is 1.9fold lower than wild-type value
W274K
-
more heat-tolerant than the wild-type enzyme. Mutant enzyme shows much reduced catalytic efficiencies as compared to the wild-type enzyme. kcat/KM is 30.6fold lower than wild-type value
A221D
mutation results in no significant alteration in activity or thermal stability
K422E
kcat value is reduced in the absence of chloride ions, and variant shows less active site heat stability
K422L
kcat value is reduced in the absence of chloride ions, and variant shows less active site heat stability
K422L/Y423F
kcat value is reduced in the absence of chloride ions, and variant shows less active site heat stability
W274A
mutation renders the enzyme about 4fold less sensitive to cyclohexylamine
W274H
mutation renders the enzyme about 4fold less sensitive to cyclohexylamine
W274K
mutation renders the enzyme about 4fold less sensitive to cyclohexylamine
Y222P
mutant displays a considerable decrease in the active site thermal stability
Y423F
kcat value is reduced in the absence of chloride ions, and variant shows less active site heat stability
F355W
-
the mutant shows slightly reduced catalytic efficiency compared to the wild type enzyme
R336L
-
the mutant shows extreme thermo-instability and its activity drops by half at 0.1 M of urea within 1.5 h
W155F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W274F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W301F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W460F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W460Y
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W475F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
additional information
D101S
weaker phosphate binding can be attributed to the increased flexibility of the Arg166 side chain, faster phosphate release is responsible for the 35fold higher activity
D101S
-
kcat value 5 to 8 times that of the wild-type with substrate 6,8-difluoro-4-methylumbelliferyl phosphate, and kcat value 9 to 17 times that of the wild-type with substrate methylumbelliferyl phosphate
D153G
-
the mutant has 5fold higher catalytic activity but no change in Km at pH 8.0 in 50 mM Tris-HCl. The mutation also affects Mg2+ binding, resulting in an enzyme with lower metal affinity. The mutation also affects the position of the water ligands of Mg2+ and the loop Gln152-Thr155 is shifted by 0.3 A away from the active site. The weaker Mg2+ binding of the mutant compared with the wild type is caused by an altered coordination sphere in the proximity of the Mg2+ ion and also by the loss of an electrostatic interaction, Mg2+/COO-Asp153, in the mutant
D153G
weaker phosphate binding can be attributed to the increased flexibility of the Arg166 side chain, faster phosphate release is responsible for the 5fold higher activity, reduced magnesium affinity, maximal activity is only achieved with the addition of exogenous magnesium
D369N
-
mutant enzyme shows reduced turnover rates and increased Km-value. The reaction mechanism of the mutant enzyme involves only 1 metal with the possible assistance of a His side chain
K328A
the mutant shows 840fold decreased catalytic efficiency compared to the wild type enzyme
R166A
mutation has very little effect on turnover number, in presence of phosphate acceptor the substrate binding decreases over 50fold, phosphate inhibition is reduced 50fold
R166S
mutation has very little effect on turnover number, in presence of phosphate acceptor the substrate binding decreases over 50fold, phosphate inhibition is reduced 50fold
R166S
kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 100000, (3-nitrobenzyl phosphate): 2300, (methyl phosphate): 110, (methyl 4-nitrophenyl phosphate): 0.48, (bis-4-nitrophenyl phosphate): 0.05, (4-nitrophenyl sulfate): 0.000058
R166S
the mutant shows 6300fold decreased catalytic efficiency compared to the wild type enzyme
R166S/E322Y
kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 1.6, (3-nitrobenzyl phosphate): below 0.2, (methyl phosphate): not determined, (methyl 4-nitrophenyl phosphate): 0.24, (bis-4-nitrophenyl phosphate): 0.021, (4-nitrophenyl sulfate): below 0.000001
R166S/E322Y
the mutant shows 39000000fold decreased catalytic efficiency compared to the wild type enzyme
additional information
-
gene disruption reveals that it is the sole alkaline phosphatase in Campylobacter jejuni
additional information
-
substitution of the conserved twin-arginine residues near the N-terminus show that they are essential for enzyme activity
additional information
alkaline phosphatase is subject to circular permutation with its novel termini at the loops near the active site, and the original termini are linked by a flexible linker. While a permutant with the termini at original residues 407 and 408 is not active, a permutant with termini at residues 90 and 94 shows significant activity. Also the addition of a randomized residue at position 91 and 93 as well as outer peptide epitopes yields several mutants with specific activity comparable to the wild-type enzyme with similar outer peptides
additional information
-
alkaline phosphatase is subject to circular permutation with its novel termini at the loops near the active site, and the original termini are linked by a flexible linker. While a permutant with the termini at original residues 407 and 408 is not active, a permutant with termini at residues 90 and 94 shows significant activity. Also the addition of a randomized residue at position 91 and 93 as well as outer peptide epitopes yields several mutants with specific activity comparable to the wild-type enzyme with similar outer peptides
additional information
the results show that the role of the arginine side chain extends beyond its positive charge, as the Arg166Lys mutant is as compromised in activity as Arg166Ser. Through measurement of individual reaction steps, a free energy profile for the hydrolysis of the enzyme-phosphate intermediate is constructed. This analysis indicates that the arginine side chain strengthens binding by approximately 3 kcal/mol and provides an additional 1-2 kcal/mol stabilization of the chemical transition state
additional information
-
the results show that the role of the arginine side chain extends beyond its positive charge, as the Arg166Lys mutant is as compromised in activity as Arg166Ser. Through measurement of individual reaction steps, a free energy profile for the hydrolysis of the enzyme-phosphate intermediate is constructed. This analysis indicates that the arginine side chain strengthens binding by approximately 3 kcal/mol and provides an additional 1-2 kcal/mol stabilization of the chemical transition state
additional information
mutant D153G/D330N lacking the signal peptide shows about 1600fold increase in activity compared to wild-type upon expression in Bacillus subtilis
additional information
HaALP is identified in the target insect gut brush border membrane vesicles as a receptor of the Bacillus thuringiensis coded Cry1Ac toxin. Lectin-ligand immunoblot assay detects the presence of alpha-GalNAc residue at the nonreducing terminal of the glycan structure in the membrane bound HaALP protein which mediates the toxin-receptor interaction
additional information
HaALP is identified in the target insect gut brush border membrane vesicles as a receptor of the Bacillus thuringiensis coded Cry1Ac toxin. Lectin-ligand immunoblot assay detects the presence of alpha-GalNAc residue at the nonreducing terminal of the glycan structure in the membrane bound HaALP protein which mediates the toxin-receptor interaction
additional information
-
HaALP is identified in the target insect gut brush border membrane vesicles as a receptor of the Bacillus thuringiensis coded Cry1Ac toxin. Lectin-ligand immunoblot assay detects the presence of alpha-GalNAc residue at the nonreducing terminal of the glycan structure in the membrane bound HaALP protein which mediates the toxin-receptor interaction
additional information
-
characterization of 11 novel mutations in the tissue non-specific alkaline phosphatase gene responsible for hypophosphatasia and genotype-phenotype correlations
additional information
deletion of nine N-terminal amino acid residues in PLAP reducs its AP activity and heat stability, while deletion of 25 amino acids results in an inactive enzyme. The N-terminal amino acid deletions affect the rate of substrate catalysis (kcat), with a minor effect on the Michaelis constant
additional information
-
deletion of nine N-terminal amino acid residues in PLAP reducs its AP activity and heat stability, while deletion of 25 amino acids results in an inactive enzyme. The N-terminal amino acid deletions affect the rate of substrate catalysis (kcat), with a minor effect on the Michaelis constant
additional information
deletion of five and nine N-terminal amino acis in TNAP reduced and abolished AP activity, respectively. The N-terminal amino acid deletions affects the rate of substrate catalysis (kcat), with a minor effect on the Michaelis constant
additional information
-
deletion of five and nine N-terminal amino acis in TNAP reduced and abolished AP activity, respectively. The N-terminal amino acid deletions affects the rate of substrate catalysis (kcat), with a minor effect on the Michaelis constant
additional information
-
to determine the mineralizing ability of mutant TNAP proteins, a functional assay is developed that uses U2OS osteoblast-like cells. Expression plasmids containing TNAP mutant cDNAs are constructed and introduced into U2OS cells, which are derived from a human osteosarcoma and exhibit very low alkaline phosphatase (ALP) activity and disabled mineralization. U2OS cells, in which active TNAP cDNAs are introduced, express high ALP activity and mineralized their circumstance when they are cultured with beta-glycerophosphate. An in vitro mineralization assay of U2OS cells transfected with moderate allele cDNAs shows that approximately 35% of TNAP enzymatic activity may be the threshold value for mineralization. In addition, U2OS cells transfected with wild-type TNAP and polymorphism TNAP cDNA shows PHEX (phosphate-regulating gene with homologies to endopeptidases on the X chromosome) induction as in SaOS-2 cells
additional information
-
hydrolysis of pyrophosphate by rat aortic rings is reduced about half in aortas from mice lacking TNAP
additional information
ALP is completely inactivated in the presence of 0.2 mM N-bromosuccinimide. Inactivation of purified alkaline phosphatase by N-bromosuccinimide is dependent on modification of only one of five tryptophan residues in the enzyme. Substrate protection experiments show that the tryptophan residue is not located at the substratebinding site but is involved in the catalytic activity
additional information
-
ALP is completely inactivated in the presence of 0.2 mM N-bromosuccinimide. Inactivation of purified alkaline phosphatase by N-bromosuccinimide is dependent on modification of only one of five tryptophan residues in the enzyme. Substrate protection experiments show that the tryptophan residue is not located at the substratebinding site but is involved in the catalytic activity
additional information
-
TNAP activity increases twofold in intact aortas and in aortic homogenates from rats made uremic by feeding adenine or by 5/6 nephrectomy. Immunoblotting showsS an increase in protein abundance but there is no increase in TNAP mRNA. An increase in TNAP activity and pyrophosphate hydrolysis also occurres when aortic rings from normal rats are incubated with uremic rat plasma
additional information
-
PhoX knockout mutant shows 10fold diminished compared with wild-type
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.1
3.5
-
about 50% loss of activity of the liver enzyme after 25 min, about 85% loss of activity of the bone enzyme after 5 min
4.4
6 - 11
7 - 13
the enzyme maintains more than 80% activity after 1 h incubation at pH 7.0-13.0
7.5
stability impaired at pH 10.5. Highest stability at pH 7.5
2.1
-
0°C, 65% inactivation of the intestinal enzyme, liver enzyme is inactivated at a rate too rapid to be measured, the longer the period in acid the smaller is the percentage of reactivation attainable after returning to pH 7.2
6 - 11
the enzyme remains stable after 24 h incubation between pH 6.0 and 11.0
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 30
100
15
20 - 65
the enzyme remains stable after 24 h incubation between 20 and 65°C
22 - 47
-
at 22, 37, and 47°C, the enzyme retains 87, 57, and 40% of activity, respectively, after 6 h of incubation, which declines faster at 57 and 60°C
25
30
35
37
4 - 10
-
the enzyme keeps 67 and 43% of activity after 1 h at 10°C and 4°C, respectively
4 - 47
-
the enzyme retains at least 80% activity it is incubated for 1 h at temperature ranging from 4°C to 47°C
40
45
50
50 - 70
-
the half-lives for the enzyme incubated in saltfree buffer at 50°C, 60°C, and 70°C is determined to be 5.3 h, 7.9 min, and 1.7 min. All the salts tested show the ability to stabilize the enzyme when incubated at 70°C
51.7
53
54
-
20 min, about 45% loss of activity of the liver enzyme, about 60% loss of activity of the bone enzyme
55
56
57
58
59
60
60.2
melting temperature, mutant K422L/Y423F, presence of 0.5 M NaCl
60.6
60.8
61
62
64
65
69
-
t1/2: 6 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
70
73
-
t1/2: 4 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
75
80
90
95
additional information
30
-
the enzyme has a half-life of less than 1 min when heated at 30°C with no additional ions in the buffer
35
-
t1/2: 31 min for wild-type enzyme, 63 min for mutant enzyme H116D, 2200 min for mutant enzyme H116S/W274K
40
-
t1/2: 12 min for wild-type enzyme, 231 min for mutant enzyme W274K, 30 min for mutant enzyme H116D, 217 min for mutant enzyme H116D/W274K
45
-
t1/2: 2.3 min for wild-type enzyme, 26 min for mutant enzyme W274K, 1.1 min for mutant enzyme H116D, 96 min for mutant enzyme H116D/W274K
50
-
88% loss of activity after 55 min in glycine buffer, 72% loss of activity after 120 min in pasteurized milk
50
-
t1/2: 182 min, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction (30 min, 15 mM)
50
-
t1/2: 77 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
50
-
t1/2: 58 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
50
-
denaturation follows first order kinetics with t1/2 values ranging from 3.5 min to 57.7 min
50
-
t1/2: 0.7 min for wild-type enzyme, 6 min for mutant enzyme W274K, 0.8 min for mutant enzyme H116D, 10 min for mutant enzyme H116D/W274K
53
-
t1/2: 26 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
53
-
t1/2: 20 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
55
-
t1/2: 41 min, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction (30 min, 15 mM)
55
-
16 min, 92% inactivation of enzyme from 20 day term fetal placentae, 86% loss of activity of enzyme from anestrus control uteri, 30% inactivation of the enzyme from small intestine
55
-
t1/2: 1.2 min for mutant enzyme W274K, 0.2 min for mutant enzyme H116D, 5 min for mutant enzyme H116D/W274K
56
-
50% inactivation of the placental enzyme after 10.9 min, 50% inactivation of the liver enzyme after 16.0 min
56
-
a monoclonal antibody based capture immunoassay is used to study the kinetics of alkaline phosphatase heat denaturation in bovine milk over a range 50-60°C for 5 to 60 min using a colorimetric quantification of the enzyme activity as a reference test. A denaturation midpoint is obtained at 56°8C for a 30 min heating
56
-
50% inactivation of the placental enzyme after 23.1 min, 50% inactivation of the liver enzyme after 14.2 min
56
-
50% inactivation of the placental enzyme after 12.3 min, 50% inactivation of the liver enzyme after 18.2 min
56
-
pH 10.6, 20 min, the isoenzymes from intestine, liver/bone/kidney and from term-placenta are unstable
56
-
placental enzyme is stable, 50% inactivation of the liver enzyme after 8.2 min
56
-
50% inactivation of the placental enzyme after 8.2 min, 50% inactivation of the liver enzyme after 18.7 min
56
-
50% inactivation of the placental enzyme after 4.4 min, 50% inactivation of the liver enzyme after 7.9 min
56
-
50% inactivation of the placental enzyme after 2.3 min, 50% inactivation of the liver enzyme after 5.8 min
56
-
50% inactivation of the placental enzyme after 10.8 min, 50% inactivation of the liver enzyme after 9.0 min
56
-
t1/2: 14 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
56
-
t1/2: 12 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
56
-
50% inactivation of the placental enzyme after 2.2 min, 50% inactivation of the liver enzyme after 5.0 min
56
-
50% inactivation of the placental enzyme after 9.7 min, 50% inactivation of the liver enzyme after 3.5 min
58
-
t1/2: 84 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
58
-
t1/2: 80 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
59
-
t1/2: 7 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
59
-
t1/2: 6 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
60
-
complete inactivation after 50 min in glycine buffer, 15% loss of activity after 120 min in pasteurized milk
60
-
about 65% loss of activity after 1 h, complete loss of activity after 6 h
60
-
biphasic thermoinactivation, t1/2 of mutant enzyme os-1 is 31.7 min for the fast phase and 3.0 h for the slow phase. The wild-type enzyme shows t1/2 values of 4.8 min and 80.3 min, respectively
60
-
t1/2: 10 min, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction (30 min, 15 mM)
62
-
t1/2: 35 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
62
-
t1/2: 37 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
64
-
120 min, about 15% loss of activity of the cytolasmic isoenzyme, about 5% loss of activity of the nuclear isoenzyme
65
-
50% inactivation of the placental enzyme after 1.04 min, 50% inactivation of the liver enzyme after 1.32 min
65
-
t1/2: 24 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
65
-
t1/2: 25 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
65
-
50% inactivation of the placental enzyme after 1.2 min, 50% inactivation of the liver enzyme after 1.31 min
65
-
50% inactivation of the placental enzyme after 0.97 min, 50% inactivation of the liver enzyme after 0.92 min
65
-
50% inactivation of the placental enzyme after 0.67 min, 50% inactivation of the liver enzyme after 0.6 min
65
-
placental enzyme is stable, 50% inactivation of the liver enzyme after 1.05 min
65
-
50% inactivation of the placental enzyme after 0.76 min, 50% inactivation of the liver enzyme after 0.45 min
65
-
50% inactivation of the placental enzyme after 0.21 min, 50% inactivation of the liver enzyme after 0.32 min
65
-
50% inactivation of the placental enzyme after 0.58 min, 50% inactivation of the liver enzyme after 0.8 min
65
-
50% inactivation of the placental enzyme after 0.52 min, 50% inactivation of the liver enzyme after 0.35 min
65
-
t1/2: 2.6 min, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction (30 min, 15 mM)
65
-
50% inactivation of the placental enzyme after 0.42 min, 50% inactivation of the liver enzyme after 0.84 min
65
-
50% inactivation of the placental enzyme after 0.91 min, 50% inactivation of the liver enzyme after 0.65 min
70
-
complete inactivation after 20 min in glycine buffer, complete inactivation after 40 min in pasteurized milk
70
-
30% loss of activity after 10 min, 98% loss of activity after 20 min
75
-
addition of Co2+ after treatment with EDTA results in an enzyme that has low tolerance toward heat treatment of more than 75°C, suggesting that Co2+ destabilizes the tertiary structure of the enzyme at high temperature
80
the enzyme retains more than 60% activity at 80?C after 1 h incubation
80
-
complete inactivation after 4 min in glycine buffer, complete inactivation after 10 min in pasteurized milk
80
retains more than 50% activity after incubating for 6 h at 80ºC
90
-
10 min, pH 8.5, containing 10 mM MgCl2 and 1 mM ZnSO4, about 50% loss of activity
95
-
10 min, pH 8.5, containing 10 mM MgCl2 and 1 mM ZnSO4, aout 80% loss of activity
95
-
5 min, in absence or presence of 10 mM Mg2+, inactivation of CAPase, while IApase is relatively stable showing loss of 30% activity after 5 min and loss of 80% activity after 30 min
additional information
residual activity after after thermal inactivation at 60°C, 120 min: 2.4%
additional information
-
the thermal stabilities of the immobilized phosphatase are higher than those of the native one
additional information
enzyme gets quickly inactivated at 80°C for 15 min, exhibiting a half-life of 8 min at 70°C
additional information
-
enzyme gets quickly inactivated at 80°C for 15 min, exhibiting a half-life of 8 min at 70°C
additional information
-
Tris-HCl partly protects against heat inactivation
additional information
-
addition of lipopolysaccharide, phosphatidylethanolamine or a combination of both increases the temperature of inactivation
additional information
-
high molecular weight alkaline phosphatase is less heat and urea stable than low molecular weight alkaline phosphatase
additional information
-
low molecular weight alkaline phosphatase is more heat and urea stable than high molecular weight alkaline phosphatase
additional information
-
Mg2+ protects against thermal inactivation up to 80°C
additional information
shrimp
-
heat-labile, the enzyme is inactivated by a short rise in temperature
additional information
-
thermostability is increased 30fold by Co2+ and 23fold by Mg2+
additional information
-
Co2+ and Zn2+ increase the thernal stability by 30 and 23fold at 90°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
24 h incubation is necessary for reaching an unfolding equilibrium, dimeric enzyme does not show any sign of dissociation up to a urea concentration of 4 M
8 M urea, at 37°C, half-life of placental enzyme: 3 h. 3 M urea, half-life of the bone enzyme: 7 min
-
activity of alkaline phosphatase is not affected after 6 min of pressure treatments (206-620 MPa), regardless of the medium in which the enzyme is prepared. Increasing the processing time to 12 min significantly reduces the activity of alkaline phosphatase at 620 MPa. Circular dichroism data demonstrated a partial change in the secondary structure of ALP at 620 MPa leading to a random coil structure
-
at 3.5 mM Ca2+, the enzyme is unstable at low NaCl concentrations but its stability increases with the salt concentration. At 32 mM Ca2+ , the enzyme is rather stable even at low NaCl concentrations. Even at 4 M NaCl, the stability of the enzyme depends on the Ca2+ concentration
-
at urea concentrations below a critical value, the enzymes are only slightly and reversibly inhibited, but above this value inactivation is progressive with time and generally irreversible. The critical concentration of urea is considerably greater for intestinal phosphatase than for the kidney and liver enzyme
-
both calcium ions (in the millimolar range) and NaCl (in the molar range) are required for the stability of the enzyme
-
carbohydrate additives such as sucrose may result in a remarkable higher reduction in the kinetics of deteriorative reactions and result in a better stability
-
enzyme is partially resistant to SDS, without heat treatment 40% of the enzyme is SDS-resistant
-
improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives
loss of activity occurrs at urea concentrations below 1 M. The global structure is unfolded at urea concentrations in the range 1-3 M
-
plays an indirect but important role in stabilizing the enzyme in its most active conformations
repeated freezing and thawing in the presence of mercaptoethanol has no effect
-
requires Mg2+ and dithiothreitol for stability throughout its purification
-
sodium dodecyl sulphate at 2% (w/v) stabilises the enzyme during freezing
-
the enzyme is irreversibly transformed into an inactive dimer by low urea concentrations
-
the enzyme is more stable in reversed micelles of hexadecyltrimethylammonium bromide in cyclohexane, with 1-butanol as co-surfactant than in bulk aqueous solution at 25°C. When the enzyme is dialysed against Mn2+-free buffer it loses all the activity within 90 min in aqueous medium, but it retains approximately 72% of the initial enzymatic activity for 90 min in reversed micelles
-
urea, 3 M, 5 h, about 50% loss of activity of the liver enzyme, about 60% loss of activity of the bone enzyme. 5 M, 30 min, about 70% loss of activity of the liver enzyme, about 90% loss of activity of the bone enzyme. 6 M, 10 min, about 70% loss of activity of the liver enzyme, about 90% loss of activity of the bone enzyme
-
improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives
-
improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, buffered preparation (50% glycerol), stored for 4 years without an apparent loss of activity
-22°C, 10 mM Tris/HCl, 50 mM NaCl, 1.5 mM MgCl2, 0.2% Zwittergent 3-14, pH 8.4, stable for several weeks
-
0-4°C, 10 mM Tris/HCl, 50 mM NaCl, 1.5 mM MgCl2, 0.2% Zwittergent 3-14, pH 8.4, stable for several days
-
25°C, 25 mM MOPS buffer, pH 8.0 with 500 mM NaCl, 2 days, no loss of activity
-
4°C, 25°C or 37°C, 0.1 M Tris-HCl buffer (pH 10.5), 15 days, 50% loss of activity
Thermus sp. NTU-237
A0A1B2YKT4
the storage stabilities of the immobilized phosphatase are higher than those of the native one
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 distinct enzyme forms, CAPase 212fold and 4 isozymes of IAPase 5-87fold
-
affinity chromatography
ammonium sulfate precipitation, DEAE-cellulose column chromatography, DEAE-Sephadex gel filtration, and Sephadex G-200 gel filtration
-
buffers need to be supplemented with 0.1 mM CoCl2. If Co2+ is omitted in the lysis buffer, activity of the cell-free extracts is only about 10% of the normal value. Addition of the absent metal to these extracts restores 100% activity, after overnight incubation at 4°C
by using chromatography on DEAE-cellulose. Enzyme is purified to homogenity on Sephacryl S-200 column
-
by using HPLC separation of a intestinal homogenate two ALP peaks (rTI2A and rTI2B) are obtained
by using HPLC separation of a rat bone homogenate one peak is obtained
by using HPLC separation of a rat liver homogenate three peaks are obtained (rTL1, rTL2 and rTL3)
commercial product
crude extract is purified using ion exchange gel DEAE-32, then by filtration chromatograph through Sephadex G-200, and ion exchange gel DEAE-32
-
gel filtration chromatography using a pre-equilibrated column containing Sephadex G-150
immobilized metal ion affinity chromatography (Ni2+)
native enzyme 2882.6fold and recombinant His-tagged enzyme expressed in Escherichia coli
-
partial
purified from brush border membran versicles, using Mono Q anionic exchange liquid chromatography and size exclusion filtering
-
purified from human placental tissue extract. The purity of PLAP after a gel filtration step is above 97%
-
purified recombinant HaALP is separated into four fractions by gel filtration. Dialyzed against 50 mM Tris-HCl (pH 8.0)/2 mM MgCl2 buffer containing 3 M NaCl, one of these four fractions is activated to almost full activity
-
purified using DEAE-cellulose and Sepharose CL-6B chromatography
-
recombinant
recombinant enzyme in nclusion bodies after expression in Escherichia coli
-
recombinant from Escherichia coli
recombinant protein, purified by precipitation and immobilized metal affinity chromatography
Strep-Tactin affinity column chromatography, and Superdex 200 gel filtration
-
treatment of isolated matrix vesicles with phosphatidylinositol-phospholipase
-
use of a chitosan-metformin/NiCl2/Fe3O4 nanobiocomposite to purify alkaline phosphatase from hen's egg yolk. Purification is a fast, reusable and cost-effective method. 62% purification efficiency is obtained and the synthesized nanobiocomposite is not attached to other proteins in hen's egg yolk. A slight decrease in adsorption capacity is observed after 4 cycles
-
using a Q-Sepharose fast flow column and a Sephacryl S200 high-resolution gel-filtration column
using affinity chromatography. Typical yields for a 6-L culture are 30-40 mg of pure protein
using L-histidyldia-zobenzylphosphonic acid agarose affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
94% fragment of gene alp cDNA, functional overexpression in Escherichia coli BL21(DE3) as internally His-tagged enzyme use of continous electrophoresis procedure
-
allozyme D, ALPP, of placental enzyme form PALP, DNA and amino acid sequence determination of PALP and allozymes, comparison and analysis, substitutions from PALP to ALPP are found at P209R and E429G, subcloning in Escherichia coli XL1-blue, and expression of allozymes D, ALPP, in CHO cells
-
circularly permutated alkaline phosphatase, expression in Escherichia coli
DNA and amino acid sequence determination and analysis, expression in Escherichia coli HMS174 (DE3)
Escherichia coli alkaline phosphatase is fused to a C-terminal region of Pseudomonas sp. MIS38 lipase (PML) and examined for secretion using the Escherichia coli cells carrying the heterologous type I secretion system. PML is one of the passenger proteins of TISS and contains 12 repetitive sequences and a secretion signal at the C-terminal region. The fusion protein is efficiently secreted to the extracellular medium, while alkaline phosphatase is not secreted at all, indicating that the secretion of alkaline phosphatase is promoted by a secretion signal of Pseudomonas sp. MIS38 lipase. The fusion protein purified from the culture supernatant existed as a homodimer, like AP, and is indistinguishable from alkaline phosphatase in enzymatic properties and stability
-
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli as an N-terminal maltose binding protein (MBP) fusion construct (AP-MBP)
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in transiently transfected COS-1 cells and in stable CHO-K1 Tet-On cells
-
expressed under the control of the T7lac promoter on the expression vector pET-22b(+) in Escherichia coli BL21(DE3)
expression in Escherichia coli
expression in Escherichia coli BL21 (DE3), full-length PhoX, and a truncated form that lacks the signal peptide
expression in Escherichia coli, Escherichia faecalis, Streptococcus agalactiae or Streptococcus pyogenes
-
expression in Escherichia coli, replacing a secretion leader coding section with a N-terminal His6-tag
expression in Pichia pastoris
expression in Spodoptera frugiperda Sf9 and Trichoplusia ni BTI-Tn-5B1-4 insect cells via infection with recombinant Autographa california multiple nuclear polyhedrovirus expressing SEAP under control of the polyhedrin promotor, the recombinant enzyme expressed in the 2 different insect cell lines show differing N-glycan structures
-
expression of wild-type and mutants in several Escherichia coli strains, intragenic complementation
-
human 1.6 kb IAP cDNA is subcloned into the pIRES2-EGFP vector, and the construct thus obtained (pIRES2-IAP-EGFP) is used to transfect into IEC-6, T84, and HT-29 cell lines. Stable cell lines are selected by G418 exposure
-
liver and milk isoenzymes have similar or perhaps identical peptide structures and may be coded by the same gene
-
overexpressed in Escherichia coli and purified as a hexa-His-tagged fusion protein
overexpression in Escherichia coli BL21(DE3) as C-terminally His-tagged enzyme
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phoK is cloned and overexpressed in Escherichia coli strain BL21(DE3). The resultant Escherichia coli strain EK4 overexpress cellular activity 55times higher and secrete extracellular PhoK activity 13times higher than Sphingomonas sp. strain BSAR-1. The recombinant strain very rapidly precipitate more that 90% of input uranium in less than 2 h from alkaline solutions (pH 9) containing 0.5 to 5 mM of uranyl carbonate. In recombinant strain EK4, precipitated uranium remains cell bound. The EK4 cells exhibited a much higher loading capacity of 3.8 g uranium/g dry weight in less than 2 h compared to only 1.5 g uranium/g dry weight in more than 7 h in strain BSAR-1
single-chain Fv antibody fusion protein expressed in Escherichia coli BL21(DE3)pLysS
the placental isoenzyme is encoded by a gene identical to the gene expressed in mouse, liver, kidney, and tetracarcinoma stem cells
three gene loci seem to be involved in determining the various forms of alkaline phosphatase, one coding for the placental form, at least one coding for the intestinal forms, and at least one for the liver, bone and kidney forms
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two transgenic rabbit lines are created by pronuclear microinjection with the whey acidic protein promoter-humanTNAP minigene (WAP-hTNAP). lactating females of both lines produce biologically active human TNAP. The recombinant alkaline phosphatase is associated with the membrane of milk fat globules. Use of transgenic rabbits as bioreactors for bulk production of human tissue-nonspecific alkaline phosphatase in milk
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alkaline phosphatase is inducible and is expressed by algae under phosphorus-stress conditions. No constitutive AP enzyme is detected. Once alkaline phosphatase is produced, it is gradually released into the water, and the algae reinduces alkaline phosphatase production
enzyme expression by human dental pulp stromal cells is increased at high cell density
expression is induced at a low inorganic phosphate concentration in the culture medium
A0A196MRA0
in vivo studies show that injection of AlCl3 in male rats results in an increased expression of serum alkaline phosphatase
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in vivo studies show that injection of AlCl3 in male rats results in decreased expression of brain and liver alkaline phosphatase. Gel filtration experiments disclose a high level of high molecular weight alkaline phosphatase compared to control animals
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in vivo studies show that injection of AlCl3 in male rats results in decreased expression of brain and liver alkaline phosphatase. Gel filtration studies show a significant reduction in low molecular weight alkaline phosphatase compared to control groups
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induction of alkaline phosphatase mRNA transcription is very sensitive to phosphorus availability and population growth
Nl-sALP mRNA level is significantly higher in a fenvalerate resistant population, compared with Sus strain
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Nl-sALP mRNA level is up-regulated upon treatment with 20-hydroxyecdysone or insecticide fenvalerate
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somatic enzyme is negatively affected by oxidative stress and UVR exposure and this effect is enhanced under high temperature and low food quality
Daphnia commutata
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the enzyme is produced only when the cells are starved of phosphate. No activity can be detected when the phosphate concentration is higher than 0.1 mM, and the highest specific activity is obtained when the minimal medium is completely devoid of phosphate. When the cells are starved of phosphate, the production of the enzyme starts immediately and continues at a constant rate for at least 48 h
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there is a significant increase of enzyme activity in Staphylococcus aureus biofilm culture compared to a suspension counterpart
alkaline phosphatase is inducible and is expressed by algae under phosphorus-stress conditions. No constitutive AP enzyme is detected. Once alkaline phosphatase is produced, it is gradually released into the water, and the algae reinduces alkaline phosphatase production
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alkaline phosphatase is inducible and is expressed by algae under phosphorus-stress conditions. No constitutive AP enzyme is detected. Once alkaline phosphatase is produced, it is gradually released into the water, and the algae reinduces alkaline phosphatase production
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alkaline phosphatase is inducible and is expressed by algae under phosphorus-stress conditions. No constitutive AP enzyme is detected. Once alkaline phosphatase is produced, it is gradually released into the water, and the algae reinduces alkaline phosphatase production
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induction of alkaline phosphatase mRNA transcription is very sensitive to phosphorus availability and population growth
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induction of alkaline phosphatase mRNA transcription is very sensitive to phosphorus availability and population growth
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there is a significant increase of enzyme activity in Staphylococcus aureus biofilm culture compared to a suspension counterpart
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there is a significant increase of enzyme activity in Staphylococcus aureus biofilm culture compared to a suspension counterpart
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
incubation in 4 M urea followed by a 15fold dilution of the urea at pH 7.5 results in a 100% recovery of initial activity after 20 or 90 min
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recombinant His-tagged enzyme from inclusion bodies after expression in Escherichia coli, solubilization by 1% SDS in ddH2O from purified inclusion bodies
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refolding behavior of guanidine hydrochloride-denatured alkaline phosphatase, despite the enhanced activity recovery yield (more than 50%), both the refolding and the reactivation rate constants decrease with increasing alpha-cyclodextrin concentrations. Detergents (used in the artificial chaperone method) increase the refolding rate significantly
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
biotechnology
degradation
diagnostics
drug development
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alkaline phosphatase interacts with Bacillus thuringiensis Cry1Ac toxin in vitro. In vitro incubation of Cry1Ac toxin with the purified alkaline phosphatase results in a 43% decrease in alkaline phosphatase specific activity. When Cry1Ac toxin is supplied to the diet of caterpillars, it is efficient in decreasing larval weight gain and survival
environmental protection
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monthly analysis of the activities of particulate and soluble phosphatase for 1 year in the coastal ecosystems of the North Western Mediterranean Sea. The mean contribution of the particulate activity increases from 56% at an methyl umbelliferyl phosphate concentration of 30 microM to 77% at 0.04 microM. This particulate activity is negatively correlated with the dissolved inorganic phosphorus concentrations, dissolved organic phosphorus and total dissolved phosphorus concentrations when the activities are related to the seawater volume, chlorophyll a or the protein concentration
food industry
medicine
molecular biology
synthesis
additional information
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use of a chitosan-metformin/NiCl2/Fe3O4 nanobiocomposite to purify alkaline phosphatase from hen's egg yolk. Purification is a fast, reusable and cost-effective method. 62% purification efficiency is obtained and the synthesized nanobiocomposite is not attached to other proteins in hen's egg yolk. A slight decrease in adsorption capacity is observed after 4 cycles
agriculture
-
analysis of non-specific alkaline phosphatase activity can be used to analyze the phosphate status of the ambient environment
agriculture
-
sterilized soil supplemented with alkaline phosphatase improves the total height, dry weight, phosphate content in the stem and root of Zea mays by 3.07, 3.15, 2.35 and 1.76 fold respectively compared to control set
agriculture
phoA alone or in combination with other phosphite metabolizing gene(s) can be used as an effective ameliorating system for improving crop plants for phosphite-based fertilization and weed management strategy in the agriculture
analysis
-
CCP-2 cells are an important tool for investigation of chondrooclastogenesis/osteoclastogenesis and endochondrial ossification
analysis
-
enzyme is a potential marker for specific plasma membrane purification
analysis
-
simple, rapid, sensitive, and selective enzymatic procedures for determining zinc and magnesium based on their inhibiting and activating effects on the catalytic activity of alkaline phosphatases
analysis
-
application of intracellular alkaline phosphatase activity measurement in detection of neutrophil adherence in vitro
analysis
-
development of a simple in situ duodenal alkaline phosphatase activity assay based on the fluorogenic substrate ELF
analysis
-
ALP and fat storage are tightly linked during preadipocyte maturation. Measurement of ALP activity may be a sensitive and rapid technique for the quantification of intracellular lipid accumulation
analysis
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ALP and fat storage are tightly linked during preadipocyte maturation. Measurement of ALP activity may be a sensitive and rapid technique for the quantification of intracellular lipid accumulation
analysis
-
simple, rapid, sensitive, and selective enzymatic procedures for determining zinc and magnesium based on their inhibiting and activating effects on the catalytic activity of alkaline phosphatases
analysis
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construction o a fusion proein between the ZZ protein, two specific Fc-fragment-binding domains derived from the B-domain of SpA, and alkaline phosphatase. The ZZ-AP fusion retains full parental activities and exhibits an approximately tenfold higher sensitivity than that of ZZ-AP conjugate in enzyme-linked immunosorbent assay. The ZZ-AP fusion is a promising immunoreagent for IgG detection and a potential biolinker between antibodies and reporter enzymes. Compared with the parents, the equilibrium dissociation constant of ZZ-AP conjugate is decreased by 32% and catalytic activity is decreased by 24%
analysis
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enzyme is capable of precipitating Cu2+ from 50 ppm CuCl2 solution with 64.3% precipitation. Phosphate generated from enzyme-mediated hydrolysis of 4-nitrophenyl phosphate binds with the copper ions
analysis
-
femtoliter droplet assay based on Poisson statistics to enable an efficient acquisition of enzyme mutants with desired activities from just a few clones
analysis
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femtoliter droplet assay based on Poisson statistics to enable an efficient acquisition of enzyme mutants with desired activities from just a few clones
analysis
incorporation of the enzyme into a three-dimensional polymeric network to obtain transparent hydrogels that can be stored at room temperature and potentially used as a disposable biosensor platform for the rapid detection of inhibitors. The immobilized enzyme retains its activity, slightly increases its thermal stability and can be stored as a xerogel at room temperature without losing its properties
analysis
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sensitive and selective fluorometric method for alkaline phosphatase determination. The method is based on the regulation of enzymatically generated poly(thymine) for the preparation of copper nanoparticles (CuNPs). When alkaline phosphatase catalyzes the hydrolysis of dTTP, the polymerization to poly(thymine) by terminal deoxynucleotidyl transferase will be disabled. This prevents the formation of CuNPs and causes a drop in fluorescence. The method shows a linear response in the activity range from 0.1 to 20 U/l and a limit of quantification of 0.3 U/l
biotechnology
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the chemical modification by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives can be utilized to increase the thermostability of psychrophilic and mesophilic enzymes while retaining their high intrinsic activity or increasing their activity
biotechnology
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the chemical modification by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives can be utilized to increase the thermostability of psychrophilic and mesophilic enzymes while retaining their high intrinsic activity or increasinf their activity
biotechnology
an assay is developed for determination of the activity of the ALP using the effect of enhancement of fluorescence of the europium(III)-tetracycline 3:1 complex (Eu(3)TC). Its luminescence, peaking at 616 nm if excited at 405 nm, is enhanced by a factor of 2.5 in the presence of phosphate. Phosphate coordinates to Eu(3)TC and enhances its luminescence intensity as a result of the displacement of water from the inner coordination sphere of the central metal. The assay is performed in a time-resolved (gated) mode, which is shown to yield larger signal changes than steady-state measurement of fluorescence. The limit of detection for ALP is 4 micromol/l. Based on this scheme, a model assay for theophylline as inhibitor for ALP is developed with a linear range from 14 to 68 micromol/l of theophylline
biotechnology
the data demonstrate the potential utility of genetically engineering PhoK for the bioprecipitation of uranium from alkaline solutions
biotechnology
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alkaline phosphatase from Escherichia coli is immobilized by copolymerization with resorcinol. The phosphatase-polyresorcinol complex synthesized retains about 74% of the original enzymatic activity. On addition to soil, free enzyme is completely inactivated in 4 days, whereas the phosphatase-polyresorcinol complex is comparatively stable.Barley seed coated with the immobilized enzyme exhibits higher rhizosphere phosphatase activity. Under pot culture conditions, an increase in the soil inorganic phosphorus is detected when the seed is encapsulated with the phosphatase-polyresorcinol complex, and a positive influence on biomass and inorganic phosphorus concentration of shoot is observed
biotechnology
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a simple and fast dynamically coated capillary electrophoretic method is developed for the characterization and inhibition studies of alkaline phosphatases
degradation
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the strain is capable of detoxifying or degrading chlorpyrifos, and enzyme AP3 takes part in degradation of organophosphorus pesticides chlorpyrifos, dichlorvos, dipterex, phoxim, and triazophos
degradation
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the strain is capable of detoxifying or degrading chlorpyrifos, and enzyme AP3 takes part in degradation of organophosphorus pesticides chlorpyrifos, dichlorvos, dipterex, phoxim, and triazophos
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diagnostics
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widely used enzyme, e.g. in ELISA, enzyme-linked immunosorbent assay
diagnostics
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enzyme can be used as a marker to differentiate testicular origin azoospermia or oligospermia from ejaculatory failure, as well as ejaculatory failure and excurrent duct blockages in an inexpensive way
diagnostics
-
the enzyme is a useful marker of the sperm-rich fraction of the ejaculate
food industry
-
quantification of alkaline phosphatase by using a monoclonal antibody-based immunoassay immunoassay is appropriate for determining mild time/temperature treatment of milk and for the control of milk pasteurization
medicine
-
hypophosphatasia is caused by deficiency of activity of the tissue-nonspecific alkaline phosphatase, resulting in a defect of bone mineralization. Anchorless enzymes tagged with an acidic oligopeptide are delivered efficiently to bone and function bioactively in bone mineralization, at least in vivo. Potential advantages for use of these tagged enzymes in enzyme replacement theraphy for hypophosphatasia
medicine
-
the control of endogenous inhibitors, such as cysteine, that interfere with the ability of tissue nonspecific alkaline phosphatase to regulate calcium pyrophosphate dihydrate crystal formation and dissolution in joints could be a potential therapeutic option for calcium pyrophosphate dihydrate crystal deposition disease
medicine
-
the brush-border enzyme, IAP, has the ability to detoxify lipopolysaccharide and prevent bacterial invasion across the gut mucosal barrier. IAP expression and function are lost with starvation and maintained by enteral feeding. It is likely that the IAP silencing that occurs during starvation is a key component of the gut mucosal barrier dysfunction seen in critically ill patients
medicine
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this particular V406A mutation highlights the structural importance of the crown domain with respect to the catalytic function of TNSALP
medicine
-
a circulating factor causes pyrophosphate deficiency by regulating TNAP activity and vascular calcification in renal failure may result from the action of this factor
medicine
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a circulating factor causes pyrophosphate deficiency by regulating TNAP activity and vascular calcification in renal failure may result from the action of this factor
medicine
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TNAP is an essential component of serum calcification activity and that its role in the shotgun mechanism is to activate the serum nucleator of apatite crystal formation
medicine
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in neonatal blood plasma, soluble 5'-nucleotidase and alkaline phosphatase mediate conversion of AMP to adenosine, whereas soluble adenosine deaminase catabolizes adenosine to inosine. Newborn blood plasma demonstrates substantially higher adenosine-generating 5'-nucleotidase and alkaline phosphatase activity and lower metabolizing adenosine deaminase activity than adult plasma. Abundant alkaline phosphatase expressed on the surface of circulating neonatal neutrophils is the dominant AMPase on these cells
medicine
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alkaline phosphatase is commonly used for signal amplification in immunoassays. Elevated enzyme can interfere with contemporary, enzyme-dependent immunoassays, including DxIcTnI and DxI-hCG
medicine
in an in vitro lipopolysaccharide-induced inflammation model using IPEC-J2 cells, the mRNA expression of interleukins IL-6, IL-8, and tumor necrosis factor-a are significantly downregulated, and that of ASC amino acid transporter ASCT-2, zonula occludens protein ZO-1, and occludin CLDN-3 are significantly upregulated by a mutant D153G/D330N lacking the signal peptide, compared with lipopolysaccharide treatment
molecular biology
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analytically widely used enzyme, e.g. in ELISA, enzyme-linked immunosorbent assay
molecular biology
shrimp
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widely used in vitro, e.g. to dephosphorylate DNA or dNTPs, since the enzyme can be inactivated by a short rise in temperature
molecular biology
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the purified alkaline phosphatase removes the 5'-phosphate group of a linearized plasmid without showing DNAase activity, indicating its potential for recombinant DNA technology
molecular biology
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influence of membrane lipid environment on the activity of GPI-anchored enzymes is investigated with PLAP reconstituted by a detergent-dialysis technique in liposomes composed of palmitoyloleoylphosphatidylcholine, alone or in mixture with lipids enriched along with the protein within lipid rafts. The highest Vmax is recorded for a phosphatidylcholine/10% monosialoganglioside, while the lowest for a phosphatidylcholine/30% cholesterol mixture and for raft-mimicking 1:1:1 phosphatidylcholine/sphingolipid/cholesterol liposomes. No significant differences in Km are detected. The GPI-enzyme activity is affected by membrane curvature
molecular biology
-
relationship between extracellular pH and the release of alkaline phosphatase using stimuli affecting extracellular pH, i.e. heat shock, nigericin, salicylicacid, benzoic acid, fusicoccin, NaOH, KOH, HCl, and the Golgi apparatus inhibitor BrefeldinA is investigated. Extracellular alkaline phosphatase is a sensitive marker for cellular stimulation
molecular biology
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colchicine inhibits the dexamethasone-promoted translocation of ALP to the plasma membrane surrounding the bile canaliculus-like structure in primary cultures of fetal rat hepatocytes by disassembling microtubules and discomposing the Golgi complex
molecular biology
-
BAP may play an important role in differentiation and maturation of human B cells
synthesis
overexpression of enzyme in Escherichia coli. After 1 day of growth, when the Escherichia coli culture is near the stationary phase, high amounts of enzyme are produced but the alkaline phosphatase activity in the cell-free extract is near the background level. Further incubation of bacterial culture leads to a tremendous increase in alkaline phosphatase activity which is maximal at the 3rd day of incubation and was 48100 times higher than at the 1st day of growth. Typically, 90-140 mg of active protein is produced in 1 l of culture
synthesis
expression of PhoA in Escherichia coli by replacing a secretion leader coding section with a N-terminal His6-tag, which results in accumulation of His6-PhoA in the cytoplasm, exceeding 50% of total cellular proteins. Precipitation and immobilized metal affinity chromatography purification yield homogeneous protein, which is reactivated by dialysis into a redox buffer. The reconstituted His6-BAP exhibits high activity and the protcol can be applied for all types of DNA termini
synthesis
-
overexpression of enzyme in Escherichia coli. After 1 day of growth, when the Escherichia coli culture is near the stationary phase, high amounts of enzyme are produced but the alkaline phosphatase activity in the cell-free extract is near the background level. Further incubation of bacterial culture leads to a tremendous increase in alkaline phosphatase activity which is maximal at the 3rd day of incubation and was 48100 times higher than at the 1st day of growth. Typically, 90-140 mg of active protein is produced in 1 l of culture
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synthesis
-
expression of PhoA in Escherichia coli by replacing a secretion leader coding section with a N-terminal His6-tag, which results in accumulation of His6-PhoA in the cytoplasm, exceeding 50% of total cellular proteins. Precipitation and immobilized metal affinity chromatography purification yield homogeneous protein, which is reactivated by dialysis into a redox buffer. The reconstituted His6-BAP exhibits high activity and the protcol can be applied for all types of DNA termini
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EXTERNAL LINKS (specific for EC-Number 3.1.3.1)
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Release 2026.1 (March 2026)
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