Lysyl oxidase (IPR001695)

Short name: Lysyl_oxidase

Overlapping homologous superfamilies


Family relationships



Lysyl oxidase (EC: (LOX) [PMID: 8104038] is an extracellular copper-dependent enzyme that catalyses the oxidative deamination of peptidyl lysine residues in precursors of various collagens and elastins, yielding alpha-aminoadipic-delta-semialdehyde. The deaminated lysines are then able to form semialdehyde cross-links, resulting in the formation of insoluble collagen and elastin fibres in the extracellular matrix [PMID: 1357535].

The active site of LOX resides towards the C terminus: this region also binds a single copper atom in an octahedral coordination complex involving at least 3 His residues [PMID: 1352776]. Four histidine residues are clustered in a central region of the enzyme. This region is thought to be involved in cooper-binding and is called the 'copper-talon' [PMID: 8104038].

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0005507 copper ion binding
GO:0016641 oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.