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Literature summary extracted from

  • Alcudia, J.F.; Martinez-Gonzalez, J.; Guadall, A.; Gonzalez-Diez, M.; Badimon, L.; Rodriguez, C.
    Lysyl oxidase and endothelial dysfunction: mechanisms of lysyl oxidase down-regulation by pro-inflammatory cytokines (2008), Front. Biosci., 13, 2721-2727.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.13 beta-aminopropionitrile
-
 Rattus norvegicus
1.4.3.13 beta-aminopropionitrile
-
 Sus scrofa
1.4.3.13 homocysteine down-regulates LOX mRNA and transcriptional activity Rattus norvegicus
1.4.3.13 homocysteine down-regulates LOX mRNA and transcriptional activity Sus scrofa
1.4.3.13 homocysteine thiolactone
-
 Rattus norvegicus
1.4.3.13 homocysteine thiolactone
-
 Sus scrofa
1.4.3.13 low-density lipoprotein
-
 Rattus norvegicus
1.4.3.13 low-density lipoprotein
-
 Sus scrofa
1.4.3.13 additional information hypercholesterolemia down-regulates LOX expression and activity Rattus norvegicus
1.4.3.13 additional information hypercholesterolemia down-regulates LOX expression and activity Sus scrofa
1.4.3.13 tumor necrosis factor-alpha inhibits LOX mRNA transcription and LOX activity Rattus norvegicus
1.4.3.13 tumor necrosis factor-alpha inhibits LOX mRNA transcription and LOX activity Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.3.13 cytosol
-
 Rattus norvegicus 5829
-
1.4.3.13 cytosol
-
 Sus scrofa 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.3.13 Cu2+ required for activity Rattus norvegicus
1.4.3.13 Cu2+ required for activity Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.13 32000
-
 active enzyme, SDS-PAGE Rattus norvegicus
1.4.3.13 32000
-
 active enzyme, SDS-PAGE Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.13 Rattus norvegicus
-
-
-
1.4.3.13 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.4.3.13 additional information LOX suffers different posttranslational modifications including signal peptide cleavage, glycosylation, copper incorporation and formation of the lysyl-tyrosyl-quinone cofactor Rattus norvegicus
1.4.3.13 additional information LOX suffers different posttranslational modifications including signal peptide cleavage, glycosylation, copper incorporation and formation of the lysyl-tyrosyl-quinone cofactor Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.13 endothelial cell
-
 Rattus norvegicus
-
1.4.3.13 endothelial cell
-
 Sus scrofa
-
1.4.3.13 vascular smooth muscle cell
-
 Rattus norvegicus
-
1.4.3.13 vascular smooth muscle cell
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O
-
 Rattus norvegicus peptidyl-allysyl-peptide + NH3 + H2O2
-
 ?
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O
-
 Sus scrofa peptidyl-allysyl-peptide + NH3 + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.3.13 LOX
-
 Rattus norvegicus
1.4.3.13 LOX
-
 Sus scrofa
1.4.3.13 lysyl oxidase
-
 Rattus norvegicus
1.4.3.13 lysyl oxidase
-
 Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.13 lysyl-tyrosyl-quinone
-
 Rattus norvegicus
1.4.3.13 lysyl-tyrosyl-quinone
-
 Sus scrofa