ExplorEnz: EC 3.4.24.34

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3.4.24.34

Accepted name:

neutrophil collagenase

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

Other name(s):

matrix metalloproteinase 8; PMNL collagenase; MMP-8

Comments:

Similar to interstitial collagenase in specificity, but the product of a different gene and highly glycosylated. Stored in the specific granules of neutrophil leukocytes. In peptidase family M10 (interstitial collagenase family). Formerly included in EC 3.4.24.7

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9001-12-1

References:

1.	Hasty, K. A., Jeffrey, J. J., Hibbs, M. S. and Welgus, H. G. The collagen substrate specificity of human neutrophil collagenase. J. Biol. Chem. 262 (1987) 10048–10052. [PMID: 3038863]
2.	Hasty, K. 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 (1990) 11421–11424. [PMID: 2164002]
3.	Knäuper, V., Krämer, S., Reinke, H. and Tschesche, H. 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 (1990) 295–300. [DOI] [PMID: 2159879]

[EC 3.4.24.34 created 1992]