Lysyl oxidase: Difference between revisions
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'''Lysyl oxidase''' is an extracellular [[enzyme]] that catalyzes formation of [[aldehydes]] from [[lysine]] residues in [[collagen]] and [[elastin]] precursors and is encoded by '' | '''Lysyl oxidase''' is an extracellular [[enzyme]] that catalyzes formation of [[aldehydes]] from [[lysine]] residues in [[collagen]] and [[elastin]] precursors and is encoded by ''LOX'' gene. These aldehydes are highly reactive, and undergo spontaneous chemical reactions with other lysyl oxidase-derived aldehyde residues, or with unmodified lysine residues. This results in [[cross-linking]] collagen and elastin, which is essential for stabilization of collagen fibrils and for the integrity and elasticity of mature elastin. | ||
Complex cross-links are formed in collagen (pyrodininolines derived from three lysine residues) and in elastin (desmosines derived from four lysine residues) that differ in structure. | Complex cross-links are formed in collagen (pyrodininolines derived from three lysine residues) and in elastin (desmosines derived from four lysine residues) that differ in structure. | ||
Revision as of 21:04, 10 November 2015
| lysyl oxidase | |
|---|---|
| Identifiers | |
| Symbol | LOX |
| Entrez | 4015 |
| HUGO | 6664 |
| OMIM | 153455 |
| RefSeq | NM_002317 |
| UniProt | P28300 |
| Other data | |
| EC number | 1.4.3.13 |
| Locus | Chr. 5 q23.3-31.2 |
Lysyl oxidase is an extracellular enzyme that catalyzes formation of aldehydes from lysine residues in collagen and elastin precursors and is encoded by LOX gene. These aldehydes are highly reactive, and undergo spontaneous chemical reactions with other lysyl oxidase-derived aldehyde residues, or with unmodified lysine residues. This results in cross-linking collagen and elastin, which is essential for stabilization of collagen fibrils and for the integrity and elasticity of mature elastin.
Complex cross-links are formed in collagen (pyrodininolines derived from three lysine residues) and in elastin (desmosines derived from four lysine residues) that differ in structure.
The importance of lysyl oxidase-derived cross-linking was established from animal studies in which lysyl oxidase was inhibited either by nutritional copper-deficiency or by supplementation of diets with β-aminopropionitrile (BAPN), an inhibitor of lysyl oxidase. This resulted in lathyrism, characterized by poor bone formation and strength, hyperextensible skin, weak ligaments, and increased occurrence of aortic aneurysms. These abnormalities correlated well with decreased cross-linking of collagen and elastin.
References
- Molecular Biology of the Cell - Alberts (2002 - 4th Edition) ISBN 0815332181
See also
External links
- Lysyl+Oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)