Conserved Site

Lysyl oxidase, conserved site (IPR019828)

Short name: Lysyl_oxidase_CS

Description

Lysyl oxidase (EC:1.4.3.13) (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].

LOX binds a single copper atom which seems to reside within an octahedral coordination complex which includes at least three histidine ligands. 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]. The signature pattern for this entry covers the four histidines that make up the putative 'copper-binding-talon'.

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.
PROSITE patterns