|PROSITE documentation PDOC00716|
Lysyl oxidase (EC 22.214.171.124) (LOX)  is an extracellular copper-dependent enzyme that catalyzes the oxidative deamination of peptidyl lysine residues in precursors of various collagens and elastins. The deaminated lysines are then able to form aldehyde cross-links.
In vertebrates LOX belongs to a family  that also includes three LOX-like proteins (genes LOXL1, LOXL2 and LOXL3) whose function is not yet known. A LOX-type catalytic domain is found in all three LOX-like proteins. LOXL2 and LOXL3 also contains 4 SRCR domains (see <PDOC00348>).
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' . We have used this region as a signature pattern.Last update:
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Krebs C.J. Krawetz S.A.|
|Title||Lysyl oxidase copper-talon complex: a model.|
|Source||Biochim. Biophys. Acta 1202:7-12(1993).|
|2||Authors||Maki J.M. Kivirikko K.I.|
|Title||Cloning and characterization of a fourth human lysyl oxidase isoenzyme.|
|Source||Biochem. J. 355:381-387(2001).|