Neutrophilic collagenase
Neutrophilic collagenase Neutrophil collagenase | |||||||||
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Identifier | |||||||||
EC number | 3.4.24.34 | ||||||||
CAS registration number | 2593923 | ||||||||
Database | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structure | RCSB PDB PDBe PDBj PDBsum | ||||||||
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The neutrophilic collagenase (Neutrophil collagenase, EC 3.4.24.34) is matrix metalloproteinase 8, the enzyme which is called PMNL collagenase, MMP-8 [1]; [2] [3]. I catalyze the following chemical reactions.
- I cut a triple spiral domain of the stroma-related collagen. Unlike stroma-related collagenase (EC 3.4.24.7), this enzyme cuts collagen of the type III than type I collagen more slowly.
In the peptidase family, I belong to M10.
Allied item
Source
- ^ 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. and 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.
Outside link
- Neutrophil collagenase - the US National Library of Medicine Medical Subject Headings (MeSH)
This article is taken from the Japanese Wikipedia Neutrophilic collagenase
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