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Neutrophil collagenase
| Field | Value |
|---|---|
| Name | Neutrophil collagenase |
| EC_number | 3.4.24.34 |
| CAS_number | 2593923 |
Neutrophil collagenase (, matrix metalloproteinase 8, PMNL collagenase, MMP-8) is an enzyme. 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.
References
References
- (July 1987). "The collagen substrate specificity of human neutrophil collagenase". The Journal of Biological Chemistry.
- (July 1990). "Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases". The Journal of Biological Chemistry.
- (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.
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