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

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 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.

External links

This article is issued from Wikipedia - version of the Monday, January 25, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.