Lysyloxidase

• OMIM: 153455
• UniProt: P28300

Lysyl oxidase, also known as the Protein -lysine 6- oxidase, is an enzyme found primarily in the extracellular space of the connective tissue of vertebrates. It catalyzes the cross-linking of collagen and elastin, thus these proteins are mechanically stabilized. In humans, copper deficiency and mutations in the LOX gene to reduce the enzyme activity, and this cause cutis laxa.

Description

Lysyl oxidase has an important role in the extracellular space at the cross-linking of collagen molecules. It catalyzes the synthesis of carbonyl groups of collagens, which form a covalent cross-linking in an aldol condensation. Lysyl oxidase thus creates the chemical conditions for the formation of fibrils.

Lysyl oxidase LOX is encoded by the gene. This gene is located on chromosome 5 in humans locus q23.3 - q31.2. The gene product ( pre-pro - lysyl oxidase ) is immediately after the translation intracellularly a molar mass of 47 kDa. By glycosylation it rises to 50 kDa. After secretion into the extracellular space, the pre-pro - lysyl oxidase is extracellularly cleaved by the bone morphogenetic protein 1 in two fragments: heavy in the 32 kDa and lysyl oxidase in a 18 kDa propeptide.