| Post Translational Modifications | The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. Proteolytically cleaved by BMP1 which removes the propeptide. Also proteolytically cleaved by ADAMTS2 and ADAMTS14, but not by ADAMTS3, at an additional cleavage site downstream of the BMP1 cleavage site. The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin. Cleavage by BMP1 to remove the propeptide does not increase enzymatic activity but increases binding to collagen. Cleavage by ADAMTS2 produces a form with reduced collagen-binding activity. Sulfated at Tyr-187 and also at either Tyr-183 or Tyr-184 which enhances binding to collagen. |
| Function | Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture. |
| Protein Name | Protein-Lysine 6-OxidaseLysyl Oxidase Cleaved Into - Protein-Lysine 6-Oxidase - Long Form - Protein-Lysine 6-Oxidase - Short Form |
| Database Links | Reactome: R-HSA-1566948Reactome: R-HSA-2243919 |
| Cellular Localisation | SecretedExtracellular Space |
| Alternative Protein Names | Protein-Lysine 6-Oxidase proteinLysyl Oxidase Cleaved Into - Protein-Lysine 6-Oxidase - Long Form - Protein-Lysine 6-Oxidase - Short Form proteinLOX protein |
Information sourced from Uniprot.org
