General Stability | Organism |
---|---|
enzyme is resistant to high urea concentrations | Homo sapiens |
enzyme is resistant to high urea concentrations | Rattus norvegicus |
enzyme is resistant to high urea concentrations | Bos taurus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic mechanism | Homo sapiens | |
additional information | - |
additional information | kinetic mechanism | Rattus norvegicus | |
additional information | - |
additional information | kinetic mechanism | Bos taurus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | inactive proenzyme proLO is secreted | Homo sapiens | - |
- |
extracellular | inactive proenzyme proLO is secreted | Bos taurus | - |
- |
extracellular | inactive proenzyme proLO is secreted into the medium of cell culture | Rattus norvegicus | - |
- |
Golgi apparatus | passage of unprocessed proenzyme | Homo sapiens | 5794 | - |
Golgi apparatus | passage of unprocessed proenzyme | Rattus norvegicus | 5794 | - |
Golgi apparatus | passage of unprocessed proenzyme | Bos taurus | 5794 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | enzyme has a copper-binding domain, copper-cofactor is required, tightly bound at the active site, may play a conformational role in the initial half-reaction | Homo sapiens | |
Cu2+ | enzyme has a copper-binding domain, copper-cofactor is required, tightly bound at the active site, may play a conformational role in the initial half-reaction | Rattus norvegicus | |
Cu2+ | enzyme has a copper-binding domain, copper-cofactor is required, tightly bound at the active site, may play a conformational role in the initial half-reaction | Bos taurus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28000 | - |
x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE | Homo sapiens |
32000 | - |
x * 32000, active enzyme, SDS-PAGE | Bos taurus |
32000 | - |
x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE | Rattus norvegicus |
46000 | - |
x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE | Homo sapiens |
50000 | - |
x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Rattus norvegicus | enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments | ? | - |
? | |
additional information | Bos taurus | enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments | ? | - |
? | |
additional information | Homo sapiens | enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments, enzyme expression in downregulated in Menkes disease, a disorder of copper transport | ? | - |
? | |
peptidyl-L-lysyl-peptide + O2 + H2O | Homo sapiens | enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates | peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? | |
peptidyl-L-lysyl-peptide + O2 + H2O | Rattus norvegicus | enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates | peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? | |
peptidyl-L-lysyl-peptide + O2 + H2O | Bos taurus | enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates | peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
4 isozymes | - |
Homo sapiens | - |
lysyl oxidase LO and several lysyloxidase-like proteins LOXL1-4 | - |
Rattus norvegicus | - |
lysyl oxidase LO and several lysyloxidase-like proteins LOXL | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | 2 NRT-consensus sequences for N-glycosylation | Homo sapiens |
glycoprotein | 2 NRT-consensus sequences for N-glycosylation | Rattus norvegicus |
glycoprotein | 2 NRT-consensus sequences for N-glycosylation | Bos taurus |
proteolytic modification | enzyme contains a catalysis-suppressing propeptide signal domain at the N-terminus | Homo sapiens |
proteolytic modification | proenzyme proLO contains a catalysis-suppressing domain and an N-terminal signal peptide | Bos taurus |
proteolytic modification | proenzyme proLO contains a catalysis-suppressing domain, cleavage site is Gly162-Asp163, and an N-terminal signal peptide, cleavage site is Cys21-Ala22, cleavage of the proenzyme domain by metalloendoprotease procollagen C-proteinase | Rattus norvegicus |
Purification (Comment) | Organism |
---|---|
from aorta, to homogeneity, solubilization from connective tissue by 4-6 M urea | Bos taurus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2 | ping-pong mechanism of 2 half-reactions completing the catalytic cycle, overview | Homo sapiens | |
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2 | ping-pong mechanism of 2 half-reactions completing the catalytic cycle, overview | Rattus norvegicus | |
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2 | ping-pong mechanism of 2 half-reactions completing the catalytic cycle, overview | Bos taurus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
aorta | - |
Bos taurus | - |
connective tissue | - |
Homo sapiens | - |
connective tissue | - |
Rattus norvegicus | - |
connective tissue | - |
Bos taurus | - |
fibroblast | secretion of free soluble enzyme | Homo sapiens | - |
fibroblast | secretion of free soluble enzyme | Rattus norvegicus | - |
fibroblast | secretion of free soluble enzyme | Bos taurus | - |
heart | - |
Homo sapiens | - |
kidney | - |
Homo sapiens | - |
liver | - |
Homo sapiens | - |
lung | - |
Homo sapiens | - |
pancreas | - |
Homo sapiens | - |
placenta | - |
Homo sapiens | - |
skeletal muscle | - |
Homo sapiens | - |
vascular smooth muscle | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
histone H1 + O2 + H2O | L-lysine residues in histone H1 | Homo sapiens | ? | - |
? | |
histone H1 + O2 + H2O | L-lysine residues in histone H1 | Rattus norvegicus | ? | - |
? | |
histone H1 + O2 + H2O | L-lysine residues in histone H1 | Bos taurus | ? | - |
? | |
additional information | enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments | Rattus norvegicus | ? | - |
? | |
additional information | enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments | Bos taurus | ? | - |
? | |
additional information | enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments, enzyme expression in downregulated in Menkes disease, a disorder of copper transport | Homo sapiens | ? | - |
? | |
additional information | enzyme contains a cytokine receptor domain, substrate specificity, preference for the L-lysine residues in the sequence N-acetyl-(Gly)4-Glu-Lys-(Gly)5-amide, enzyme is tightly associated to the substrates in connective tissue | Homo sapiens | ? | - |
? | |
additional information | enzyme contains a cytokine receptor domain, substrate specificity, preference for the L-lysine residues in the sequence N-acetyl-(Gly)4-Glu-Lys-(Gly)5-amide, enzyme is tightly associated to the substrates in connective tissue | Rattus norvegicus | ? | - |
? | |
additional information | enzyme contains a cytokine receptor domain, substrate specificity, preference for the L-lysine residues in the sequence N-acetyl-(Gly)4-Glu-Lys-(Gly)5-amide, enzyme is tightly associated to the substrates in connective tissue | Bos taurus | ? | - |
? | |
n-alkylamine + O2 + H2O | synthetic substrates | Homo sapiens | aldehyde + NH3 + H2O2 | - |
? | |
n-alkylamine + O2 + H2O | synthetic substrates | Rattus norvegicus | aldehyde + NH3 + H2O2 | - |
? | |
n-alkylamine + O2 + H2O | synthetic substrates | Bos taurus | aldehyde + NH3 + H2O2 | - |
? | |
peptidyl-L-lysyl-peptide + O2 + H2O | enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates | Homo sapiens | peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? | |
peptidyl-L-lysyl-peptide + O2 + H2O | enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates | Rattus norvegicus | peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? | |
peptidyl-L-lysyl-peptide + O2 + H2O | enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates | Bos taurus | peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? | |
peptidyl-L-lysyl-peptide + O2 + H2O | in a variatey of basic globular proteins | Homo sapiens | peptidyl-allysyl-peptide + NH3 + H2O2 | i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde | ? | |
peptidyl-L-lysyl-peptide + O2 + H2O | in a variatey of basic globular proteins | Rattus norvegicus | peptidyl-allysyl-peptide + NH3 + H2O2 | i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde | ? | |
peptidyl-L-lysyl-peptide + O2 + H2O | in a variety of basic globular proteins | Bos taurus | peptidyl-allysyl-peptide + NH3 + H2O2 | i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde | ? |
Subunits | Comment | Organism |
---|---|---|
? | x * 32000, active enzyme, SDS-PAGE | Bos taurus |
? | x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE | Homo sapiens |
? | x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE | Rattus norvegicus |
More | structural implications of primary sequence, overview | Bos taurus |
More | structural implications of primary sequence, profile of ionic residues in LO and LOXL-1, overview | Homo sapiens |
More | structural implications of primary sequence, profile of ionic residues, overview | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
LO | - |
Homo sapiens |
LO | - |
Rattus norvegicus |
lysyl oxidase | - |
Homo sapiens |
lysyl oxidase | - |
Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
lysyl-tyrosyl quinone | essential LTQ cofactor, a unique carbonyl cofactor forming an intramolecular covalent bond, autcatalytic hydroxylation and oxidation of a Tyr residue, structure overview | Bos taurus | |
lysyl-tyrosyl quinone | essential LTQ cofactor, a unique carbonyl cofactor forming an intramolecular covalent bond, Lys314 and Tyr349 are progenitors of the cofactor, autcatalytic hydroxylation and oxidation of Tyr349, structure overview | Rattus norvegicus | |
lysyl-tyrosyl quinone | essential LTQ cofactor, a unique carbonyl cofactor forming an intramolecular covalent bond, structure overview | Homo sapiens |