Neutrophil collagenase

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
Neutrophil collagenase
Identifiers
EC number3.4.24.34
CAS number2593923
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

This enzyme belongs to the peptidase family M10.

See also

References

  1. Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG (July 1987). "The collagen substrate specificity of human neutrophil collagenase". The Journal of Biological Chemistry. 262 (21): 10048–52. PMID 3038863.
  2. Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL (July 1990). "Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases". The Journal of Biological Chemistry. 265 (20): 11421–4. PMID 2164002.
  3. Knäuper V, Krämer S, Reinke H, Tschesche H (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. 189 (2): 295–300. doi:10.1111/j.1432-1033.1990.tb15489.x. PMID 2159879.
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