PROSITE documentation PDOC00716Lysyl 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 <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' [1]. We have used this region as a signature pattern.
Last update:December 2004 / Pattern and text revised.
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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). | |
| PubMed ID | 8104038 |
| 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). | |
| PubMed ID | 11284725 |
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