Neutrophil collagenase
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
| 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 | ||||||||
| |||||||||
This enzyme belongs to the peptidase family M10.
See also
References
- Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG (July 1987). "The collagen substrate specificity of human neutrophil collagenase". The Journal of Biological Chemistry. 262 (21): 10048–52. PMID 3038863.
- Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL (July 1990). "Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases". The Journal of Biological Chemistry. 265 (20): 11421–4. PMID 2164002.
- Knäuper V, Krämer S, Reinke H, Tschesche H (April 1990). "Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms". European Journal of Biochemistry. 189 (2): 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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