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Literature summary for 3.1.1.7 extracted from

  • Meirer, K.; Glatzel, D.; Kretschmer, S.; Wittmann, S.K.; Hartmann, M.; Bloecher, R.; Angioni, C.; Geisslinger, G.; Steinhilber, D.; Hofmann, B.; Fuerst, R.; Proschak, E.
    Design, synthesis and cellular characterization of a dual inhibitor of 5-lipoxygenase and soluble epoxide hydrolase (2016), Molecules, 22, 45.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene ace1, sequence comparisons and phylogenetic analysis Tetranychus urticae
gene ace1, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE1 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system Pardosa pseudoannulata
gene ace2, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE2 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system Pardosa pseudoannulata
gene ace3, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE3 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system Pardosa pseudoannulata
gene ace4, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE4 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system Pardosa pseudoannulata
gene ace5, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme PpAChE5 as EGFP-tagged protein in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system Pardosa pseudoannulata
gene ache, sequence comparisons and phylogenetic analysis Tetronarce californica

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of crystal structure PDB ID 4ey4 Tetronarce californica
analysis of crystal structure PDB ID 4ey4 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
(7R,11R)-huprine 19 huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236 Homo sapiens
(7R,11R)-huprine 19 huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236 Tetronarce californica
(7S,11S)-huprine W huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236 Homo sapiens
(7S,11S)-huprine W huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236 Tetronarce californica
BW284c51 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide; 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide; 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide; 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide; 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide Pardosa pseudoannulata
Carbaryl
-
Pardosa pseudoannulata
decamethonium decamethonium is a prototypical dual binding site ligand of AChE that spans the active site gorge from the P-site to the choline binding pocket in the A-site Homo sapiens
decamethonium decamethonium is a prototypical dual binding site ligand of AChE that spans the active site gorge from the P-site to the choline binding pocket in the A-site, where it is stabilized by the cation-Pi interactions illustrated in its complex with Torpedo californica AChE (TcAChE), binding structure, overview Tetronarce californica
diazoxon
-
Pardosa pseudoannulata
edrophonium
-
Homo sapiens
edrophonium
-
Tetronarce californica
eserine
-
Pardosa pseudoannulata
ethopropazine ethopropazine is a substituted phenothiazine with a marked specificity for BChE. The 9000fold difference in Ki between hAChE and hBChE (EC 3.1.1.8) reflects this specificity Homo sapiens
ethopropazine
-
Tetronarce californica
fenobucarb
-
Pardosa pseudoannulata
iso-ompa tetraisopropyl diphosphoramide, inhibition of activity with butyrylthiocholine Pardosa pseudoannulata
additional information determination and analysis of the crystal structures of enzyme-bound ligands Homo sapiens
additional information no inhibition of activity with butyrylthiocholine by ISO-OMPA (tetraisopropyl diphosphoramide); no inhibition of activity with butyrylthiocholine by ISO-OMPA (tetraisopropyl diphosphoramide); no inhibition of activity with butyrylthiocholine by ISO-OMPA (tetraisopropyl diphosphoramide); no inhibition of activity with butyrylthiocholine by ISO-OMPA (tetraisopropyl diphosphoramide) Pardosa pseudoannulata
additional information determination and analysis of the crystal structures of enzyme-bound ligands Tetronarce californica
paraoxon
-
Pardosa pseudoannulata
propidium
-
Homo sapiens
propidium structure of the complex is solved at 3.0 A resolution, absence involving Trp279 in TcAChE at the gorge Tetronarce californica
thioflavin T
-
Homo sapiens
thioflavin T ThT, is not sufficiently long to span the P-site and the choline binding site pocket of enzyme TcAChE. The benzothiazole and dimethylaminophenyl rings, and the dimethylamino group of this ligand are coplanar and lay parallel to Trp279 and Tyr334 and Phe330, respectively. The dimethylamino group is at 3.3 A from the aromatic ring of Phe330 but remains far from the gorge bottom, at a distance of 8.5 A from the carboxylate oxygens of Glu199. This position at the P-site allows concomitant binding of A-site ligands like edrophonium or m-(N,N,N-trimethylammonio)trifluoroacetophenone (TMTFA) through an adjustment of the orientation of Phe330 Tetronarce californica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Pardosa pseudoannulata
0.0429
-
acetylthiocholine pH 8.0, temperature not specified in the publication Pardosa pseudoannulata
0.0616
-
acetylthiocholine pH 7.5, temperature not specified in the publication Pardosa pseudoannulata
0.1986
-
butyrylthiocholine pH 8.0, temperature not specified in the publication Pardosa pseudoannulata
0.2694
-
butyrylthiocholine pH 7.5, temperature not specified in the publication Pardosa pseudoannulata
0.2793
-
propionylthiocholine pH 7.5, temperature not specified in the publication Pardosa pseudoannulata
0.5036
-
propionylthiocholine pH 8.0, temperature not specified in the publication Pardosa pseudoannulata
0.5368
-
acetylthiocholine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
0.8588
-
butyrylthiocholine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
1.1486
-
propionylthiocholine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
1.304
-
acetylthiocholine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
1.529
-
butyrylthiocholine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
1.548
-
propionylthiocholine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
4.414
-
acetylthiocholine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
4.496
-
propionylthiocholine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
4.542
-
butyrylthiocholine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetylcholine + H2O Tetronarce californica
-
choline + acetate
-
?
acetylcholine + H2O Pardosa pseudoannulata
-
choline + acetate
-
?
acetylcholine + H2O Tetranychus urticae
-
choline + acetate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P22303
-
-
Pardosa pseudoannulata A0A1B1FIV8 collected from paddy fields of Nanjing (Jiangsu, China) in September 2015
-
Pardosa pseudoannulata A0A1B1FIW0 collected from paddy fields of Nanjing (Jiangsu, China) in September 2015
-
Pardosa pseudoannulata A0A1B1FIW2 collected from paddy fields of Nanjing (Jiangsu, China) in September 2015
-
Pardosa pseudoannulata A0A1B1FIZ1 collected from paddy fields of Nanjing (Jiangsu, China) in September 2015
-
Pardosa pseudoannulata V5QQC6 collected from paddy fields of Nanjing (Jiangsu, China) in September 2015
-
Tetranychus urticae Q86CZ4
-
-
Tetronarce californica P04058 i.e. Tetronarce californica
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.08
-
about, crude recombinant enzyme, pH 8.0, temperature not specified in the publication Pardosa pseudoannulata
0.1
-
about, crude recombinant enzyme, pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
0.12
-
about, crude recombinant enzyme, pH 7.5, temperature not specified in the publication Pardosa pseudoannulata
0.23
-
about, crude recombinant enzyme, pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
0.315
-
crude recombinant enzyme, pH 7.0, temperature not specified in the publication Pardosa pseudoannulata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylcholine + H2O
-
Tetronarce californica choline + acetate
-
?
acetylcholine + H2O
-
Pardosa pseudoannulata choline + acetate
-
?
acetylcholine + H2O
-
Tetranychus urticae choline + acetate
-
?
acetylthiocholine + H2O
-
Pardosa pseudoannulata thiocholine + acetate
-
?
acetylthiocholine + H2O preferred substrate, isozyme PpAChE5 shows the highest catalytic efficiency (Vmax/KM) for substrate acetylthiocholine, which is about 5.4 and 8.6 times compared to butyrylthiocholine and propionylthiocholine, respectively Pardosa pseudoannulata thiocholine + acetate
-
?
butyrylthiocholine + H2O
-
Pardosa pseudoannulata thiocholine + butyrate
-
?
butyrylthiocholine + H2O lower activity Pardosa pseudoannulata thiocholine + butyrate
-
?
propionylthiocholine + H2O
-
Pardosa pseudoannulata thiocholine + propionate
-
?
propionylthiocholine + H2O low activity Pardosa pseudoannulata thiocholine + propionate
-
?

Synonyms

Synonyms Comment Organism
AcE1
-
Pardosa pseudoannulata
AcE1
-
Tetranychus urticae
ACE2
-
Pardosa pseudoannulata
ace3
-
Pardosa pseudoannulata
ace4
-
Pardosa pseudoannulata
ace5
-
Pardosa pseudoannulata
AChE
-
Tetronarce californica
AChE
-
Homo sapiens
AChE
-
Tetranychus urticae
AChE1
-
Pardosa pseudoannulata
AChE2
-
Pardosa pseudoannulata
AChE3
-
Pardosa pseudoannulata
AChE4
-
Pardosa pseudoannulata
AChE5
-
Tetronarce californica
hAChE
-
Homo sapiens
PpAChE5
-
Pardosa pseudoannulata
TcAChE
-
Tetronarce californica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Pardosa pseudoannulata
7.5
-
-
Pardosa pseudoannulata
8
-
-
Pardosa pseudoannulata

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information ligand dissociation constants and inhibition kinetics Tetronarce californica
0.0000736
-
BW284c51 pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
0.000245
-
eserine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
0.000624
-
eserine pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
0.00155
-
paraoxon pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
0.00164
-
diazoxon pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
0.00168
-
Carbaryl pH 7.0, temperature not specified in the publication Pardosa pseudoannulata
0.00185
-
fenobucarb pH 7.0, temperature not specified in the publication Pardosa pseudoannulata

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0000368
-
pH 8.0, temperature not specified in the publication Pardosa pseudoannulata BW284c51
0.0000512
-
pH 7.0, temperature not specified in the publication Pardosa pseudoannulata BW284c51
0.0000652
-
pH 8.0, temperature not specified in the publication Pardosa pseudoannulata eserine
0.0001167
-
pH 7.0, temperature not specified in the publication Pardosa pseudoannulata eserine
0.000471
-
pH 7.0, temperature not specified in the publication Pardosa pseudoannulata BW284c51
0.001163
-
pH 7.0, temperature not specified in the publication Pardosa pseudoannulata eserine
0.00186
-
pH 7.0, temperature not specified in the publication Pardosa pseudoannulata eserine
0.00254
-
pH 7.0, temperature not specified in the publication Pardosa pseudoannulata BW284c51
0.0217
-
pH 7.0, temperature not specified in the publication Pardosa pseudoannulata iso-ompa

General Information

General Information Comment Organism
evolution key amino acid differences at functional sites among AChEs of Torpedo californica, Tetranychus urticae, and Pardosa pseudoannulata, evolutionary relationships, overview Tetronarce californica
evolution key amino acid differences at functional sites among AChEs of Torpedo californica, Tetranychus urticae, and Pardosa pseudoannulata, evolutionary relationships, overview Pardosa pseudoannulata
evolution key amino acid differences at functional sites among AChEs of Torpedo californica, Tetranychus urticae, and Pardosa pseudoannulata, evolutionary relationships, overview Tetranychus urticae
additional information catalysis takes place in a 20-A deep active site gorge and involves a catalytic triad of serine, histidine, and glutamate residues located near the bottom of the gorge, denoted the acylation or A-site. The region near the rim of the gorge has been denoted the peripheral site or P-site Tetronarce californica
additional information catalysis takes place in a 20-A deep active site gorge and involves a catalytic triad of serine, histidine, and glutamate residues located near the bottom of the gorge, denoted the acylation or A-site. The region near the rim of the gorge has been denoted the peripheral site or P-site Homo sapiens
additional information the catalytic triad is formed by residues S200, E327, and H440 Tetronarce californica
additional information the catalytic triad is formed by Ser, Glu, and His residues Pardosa pseudoannulata
additional information the catalytic triad is formed by Ser, Glu, and His residues Tetranychus urticae
physiological function acetylcholinesterase (AChE) is an important neurotransmitter hydrolase in invertebrate and vertebrate nervous systems. The number of AChEs is various among invertebrate species, with different functions including the classical role in terminating synaptic transmission and other non-classical roles Tetronarce californica
physiological function acetylcholinesterase (AChE) is an important neurotransmitter hydrolase in invertebrate and vertebrate nervous systems. The number of AChEs is various among invertebrate species, with different functions including the classical role in terminating synaptic transmission and other non-classical roles Pardosa pseudoannulata
physiological function acetylcholinesterase (AChE) is an important neurotransmitter hydrolase in invertebrate and vertebrate nervous systems. The number of AChEs is various among invertebrate species, with different functions including the classical role in terminating synaptic transmission and other non-classical roles Tetranychus urticae