{PDOC00716} {PS00926; LYSYL_OXIDASE} {BEGIN} ********************************************************** * Lysyl oxidase putative copper-binding region signature * ********************************************************** Lysyl oxidase (EC 1.4.3.13) (LOX) [1] 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 [2] 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 ). 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' [1]. We have used this region as a signature pattern. -Consensus pattern: W-x-W-H-x-C-H-x-H-[YN]-H-S-[MI]-[DE] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2004 / Pattern and text revised. [ 1] Krebs C.J., Krawetz S.A. "Lysyl oxidase copper-talon complex: a model." Biochim. Biophys. Acta 1202:7-12(1993). PubMed=8104038 [ 2] Maki J.M., Kivirikko K.I. "Cloning and characterization of a fourth human lysyl oxidase isoenzyme." Biochem. J. 355:381-387(2001). PubMed=11284725 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}