Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. In addition to cross linking of extracellular matrix proteins, it may have a direct role in tumor suppression. H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+) Contains 1 lysine tyrosylquinone. Increases between day 8 and 16 of embryonic development, during aortic embryogenesis, in direct proportion to total protein synthesis. 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 (By similarity). Also proteolytically cleaved by ADAMTS2 and ADAMTS14, but not by ADAMTS3, at an additional cleavage site downstream of the BMP1 cleavage site (By similarity). The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin (By similarity). Cleavage by BMP1 to remove the propeptide does not increase enzymatic activity but increases binding to collagen (By similarity). Cleavage by ADAMTS2 produces a form with reduced collagen-binding activity (By similarity). Sulfated at Tyr-190 and also at either Tyr-186 or Tyr-187 which enhances binding to collagen. Belongs to the lysyl oxidase family.