Lysyl oxidase
mammalian protein found in Homo sapiens

Lysyl oxidase (LOX), also known as protein-lysine 6-oxidase, is an enzyme that, in humans, is encoded by the LOX gene. It catalyzes the conversion of lysine residues into its aldehyde derivative allysine. Allysine form cross-links in extracellular matrix proteins. Inhibition of lysyl oxidase can cause osteolathyrism, but, at the same time, its upregulation by tumor cells may promote metastasis of the existing tumor, causing it to become malignant and cancerous.
Structure
In the yeast species Pichia pastoris, lysyl oxidase constitutes a homodimeric structure. Each monomer consists of an active site that includes a Cu(II) atom, coordinated by three histidine residues, as well as 2,4,5-trihydroxyphenylalanine quinone (TPQ), a crucial cofactor.
In humans, the LOX gene is located on chromosome 5 q23.3-31.2. The DNA sequence encodes a polypeptide of 417 amino acids, the first 21 residues of which constitute a signal peptide, with a weight of approximately 32 kDa. The carboxyterminus contains the active copper (II) ion, lysine, tyrosine, and cysteine residues that comprise the catalytically active site. The three-dimensional structure of human lysyl oxidase has not yet been resolved.
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