Neutrophil collagenase explained

Neutrophil collagenase
Ec Number:	3.4.24.34
Cas Number:	2593923

Neutrophil collagenase (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

• Collagenase

Notes and References

1. Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG . The collagen substrate specificity of human neutrophil collagenase . The Journal of Biological Chemistry . 262 . 21 . 10048–52 . July 1987 . 3038863 .
2. Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL . Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases . The Journal of Biological Chemistry . 265 . 20 . 11421–4 . July 1990 . 2164002 .
3. Knäuper V, Krämer S, Reinke H, Tschesche H . 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 . April 1990 . 2159879 . 10.1111/j.1432-1033.1990.tb15489.x . free .