Neutrophil collagenase
| Neutrophil collagenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.34 | ||||||||
| CAS number | 2593923 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Neutrophil collagenase (EC 3.4.24.34, matrix metalloproteinase 8, PMNL collagenase, MMP-8) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, interstitial collagenase, this enzyme cleaves type III collagen more slowly than type I
This enzyme belongs to the peptidase family M10.
See also
References
- ↑ Hasty, K. (1987). "A., Jeffrey, J. J., Hibbs, M. S. and Welgus, H. G. The collagen substrate specificity of human neutrophil collagenase". J. Biol. Chem. 262 (21): 10048–10052. PMID 3038863.
- ↑ Hasty, K. (1990). "A., Pourmotabbed, T. F., Goldberg, G. I., Thompson, J. P., Spinella, D. G., Stevens, R. M. and Mainardi, C. L. Human Neutrophil Collagenase. A distinct gene product with homology to other matrix metalloproteinases". J. Biol. Chem. 265 (20): 11421–11424. PMID 2164002.
- ↑ Knäuper, V.; Krämer, S.; Reinke, H.; Tschesche, H. (1990). "Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence and determination of the proenzyme and various proteolytically activated forms". Eur. J. Biochem. 189: 295–300. doi:10.1111/j.1432-1033.1990.tb15489.x. PMID 2159879.
External links
- Neutrophil collagenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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