EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.13 | beta-aminopropionitrile | inhibition of LOXL-1 | Drosophila melanogaster | |
1.4.3.13 | beta-aminopropionitrile | selective inhibition of mammalian LOX | Homo sapiens | |
1.4.3.13 | beta-aminopropionitrile | selective inhibition of mammalian LOX | Mus musculus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.4.3.13 | extracellular matrix | LOX, LOXL | Homo sapiens | 31012 | - |
1.4.3.13 | additional information | lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 show individual, developmentally regulated tissue and cell-specific expression and localization | Mus musculus | - |
- |
1.4.3.13 | additional information | lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 show individual, developmentally regulated tissue and cell-specific expression and localization | Homo sapiens | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.13 | Cu2+ | copper-cofactor, lysyl oxidase and LOX-like proteins LOXL-1 and LOXL-2, conserved binding domain | Drosophila melanogaster | |
1.4.3.13 | Cu2+ | lysyl oxidase and LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 | Mus musculus | |
1.4.3.13 | Cu2+ | lysyl oxidase and LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.13 | additional information | Homo sapiens | LOX induced chromatin changes, mechanism via histone deamination | ? | - |
? | |
1.4.3.13 | additional information | Drosophila melanogaster | LOX induced chromatin changes, mechanism via histone deamination | ? | - |
? | |
1.4.3.13 | peptidyl-L-lysyl-peptide + O2 + H2O | Mus musculus | - |
peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? | |
1.4.3.13 | peptidyl-L-lysyl-peptide + O2 + H2O | Homo sapiens | - |
peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? | |
1.4.3.13 | peptidyl-L-lysyl-peptide + O2 + H2O | Drosophila melanogaster | - |
peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.3.13 | Drosophila melanogaster | Q9N9Y8 | LOXL-2; lysyl oxidase and 2 LOX-like proteins LOXL and LOXL2 | - |
1.4.3.13 | Drosophila melanogaster | Q9V9X5 | LOXL-1; lysyl oxidase and 2 LOX-like proteins LOXL and LOXL2 | - |
1.4.3.13 | Homo sapiens | - |
structurally and functionally diverse enzyme forms: lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4, probably existing splicing variants of LOXL3 | - |
1.4.3.13 | Mus musculus | - |
adult B6SJLF1 mice, structurally and functionally diverse enzyme forms: lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4, probably existing splicing variants of LOXL3 | - |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
1.4.3.13 | proteolytic modification | N-terminal processing by BMP-1 of lysyl oxidase and LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 in the extracellular matrix results in active proteins | Mus musculus |
1.4.3.13 | proteolytic modification | N-terminal processing by BMP-1 of lysyl oxidase and LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 in the extracellular matrix results in active proteins | Homo sapiens |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.4.3.13 | aorta | LOX, LOXL, LOXL3, low expression level of LOXL2 | Homo sapiens | - |
1.4.3.13 | embryo | LOXL-1 | Drosophila melanogaster | - |
1.4.3.13 | embryo | LOXL-1, no expression of LOXL-2 | Drosophila melanogaster | - |
1.4.3.13 | heart | only in fetal heart, LOXL2, very low expression level of LOXL3 | Homo sapiens | - |
1.4.3.13 | kidney | LOXL4, LOX, LOXL | Homo sapiens | - |
1.4.3.13 | larva | LOXL-1 | Drosophila melanogaster | - |
1.4.3.13 | larva | LOXL-1, no expression of LOXL-2 | Drosophila melanogaster | - |
1.4.3.13 | lung | LOXL4, LOX, LOXL | Homo sapiens | - |
1.4.3.13 | additional information | adult fly: LOXL and LOXL-2, the latter occurs exclusively in adult flies, developmental expression analysis of LOX-like proteins LOXL and LOXL2 in embryos, larvae, pupae, and adult flies, no expression of LOXL-2 in larvae, pupae, and embryos, overview | Drosophila melanogaster | - |
1.4.3.13 | additional information | adult fly: LOXL and LOXL-2, the latter occurs exclusively in adult flies, developmental expression analysis of LOX-like proteins LOXL and LOXL2 in embryos, larvae, pupae, and adult flies, overview | Drosophila melanogaster | - |
1.4.3.13 | additional information | lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 show individual, developmentally regulated tissue and cell-specific expression and localization | Mus musculus | - |
1.4.3.13 | additional information | lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 show individual, developmentally regulated tissue and cell-specific expression and localization, expression patterns, LOX and LOXL are expressed in most tissues | Homo sapiens | - |
1.4.3.13 | ovary | LOXL4, LOX, LOXL | Homo sapiens | - |
1.4.3.13 | pancreas | LOXL4, LOX, LOXL | Homo sapiens | - |
1.4.3.13 | placenta | LOXL4, LOXL2, LOX, LOXL | Homo sapiens | - |
1.4.3.13 | prostate | LOXL2, LOX, LOXL | Homo sapiens | - |
1.4.3.13 | pupa | LOXL-1 | Drosophila melanogaster | - |
1.4.3.13 | pupa | LOXL-1, no expression of LOXL-2 | Drosophila melanogaster | - |
1.4.3.13 | testis | LOXL4, LOX, LOXL | Homo sapiens | - |
1.4.3.13 | uterus | LOXL2, LOX, LOXL | Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.13 | additional information | LOX induced chromatin changes, mechanism via histone deamination | Homo sapiens | ? | - |
? | |
1.4.3.13 | additional information | LOX induced chromatin changes, mechanism via histone deamination | Drosophila melanogaster | ? | - |
? | |
1.4.3.13 | additional information | lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain a cytokine receptor-like domain | Mus musculus | ? | - |
? | |
1.4.3.13 | additional information | lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain a cytokine receptor-like domain | Homo sapiens | ? | - |
? | |
1.4.3.13 | peptidyl-L-lysyl-peptide + O2 + H2O | - |
Mus musculus | peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? | |
1.4.3.13 | peptidyl-L-lysyl-peptide + O2 + H2O | - |
Homo sapiens | peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? | |
1.4.3.13 | peptidyl-L-lysyl-peptide + O2 + H2O | - |
Drosophila melanogaster | peptidyl-allysyl-peptide + NH3 + H2O2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.4.3.13 | More | domain structure of LOX-like protein | Drosophila melanogaster |
1.4.3.13 | More | domain structure of LOX-like protein, LOXL-1 and LOXL-2 contain SRCR domains | Drosophila melanogaster |
1.4.3.13 | More | the enzymes contain SRCR domains | Homo sapiens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.3.13 | LOX | - |
Mus musculus |
1.4.3.13 | LOX | - |
Homo sapiens |
1.4.3.13 | LOX | - |
Drosophila melanogaster |
1.4.3.13 | LOX-like protein | - |
Drosophila melanogaster |
1.4.3.13 | LOXL | - |
Mus musculus |
1.4.3.13 | LOXL | - |
Homo sapiens |
1.4.3.13 | LOXL | - |
Drosophila melanogaster |
1.4.3.13 | lysyl oxidase | - |
Mus musculus |
1.4.3.13 | lysyl oxidase | - |
Homo sapiens |
1.4.3.13 | lysyl oxidase | - |
Drosophila melanogaster |
1.4.3.13 | lysyl oxidase-like protein | - |
Mus musculus |
1.4.3.13 | lysyl oxidase-like protein | - |
Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.13 | quinone | lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain conserved lysyl and tyrosyl residues that may contribute to quinone cofactor formation | Mus musculus | |
1.4.3.13 | quinone | lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain conserved lysyl and tyrosyl residues that may contribute to quinone cofactor formation | Homo sapiens |