Gelatinase A

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Gelatinase A
Gelatinase A, Human
EC no.
CAS no.146480-35-5
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

Gelatinase A, also known as MMP2 (EC, 72-kDa gelatinase, matrix metalloproteinase 2, type IV collagenase, 3/4 collagenase, matrix metalloproteinase 5, 72 kDa gelatinase type A, collagenase IV, collagenase type IV, MMP 2, type IV collagen metalloproteinase, type IV collagenase/gelatinase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction

Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-Ile-Ala-Gly-Gln

This secreted endopeptidase belongs to the peptidase family M10.


  1. ^ Murphy G, McAlpine CG, Poll CT, Reynolds JJ (September 1985). "Purification and characterization of a bone metalloproteinase that degrades gelatin and types IV and V collagen". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 831 (1): 49–58. doi:10.1016/0167-4838(85)90148-7. PMID 2994741.
  2. ^ Collier IE, Wilhelm SM, Eisen AZ, Marmer BL, Grant GA, Seltzer JL, Kronberger A, He CS, Bauer EA, Goldberg GI (May 1988). "H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen". The Journal of Biological Chemistry. 263 (14): 6579–87. PMID 2834383.
  3. ^ Okada Y, Morodomi T, Enghild JJ, Suzuki K, Yasui A, Nakanishi I, Salvesen G, Nagase H (December 1990). "Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties". European Journal of Biochemistry. 194 (3): 721–30. doi:10.1111/j.1432-1033.1990.tb19462.x. PMID 2269296.

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