Gelatinase A

Gelatinase A

Gelatinase A, Human
Identifiers
EC number 3.4.24.24
CAS number 146480-35-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Gelatinase A (EC 3.4.24.24, 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.

References

  1. ↑ Murphy, G.; McAlpine, C.G.; Poll, C.T.; Reynolds, J.J. (1985). "Purification and characterization of a bone metalloproteinase that degrades gelatin and types IV and V collagen". Biochim. Biophys. Acta. 831: 49–58. PMID 2994741. doi:10.1016/0167-4838(85)90148-7.
  2. ↑ Collier, I.E.; Wilhelm, S.M.; Eisen, A.Z.; Marmer, B.L.; Grant, G.A.; Seltzer, J.L.; Kronberger, A.; He, C.; Bauer, E.A.; Goldberg, G.I. (1988). "H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen". J. Biol. Chem. 263: 6579–6587. PMID 2834383.
  3. ↑ Okada, Y.; Morodomi, T.; Enghild, J.J.; Suzuki, K.; Yasui, A.; Nakanishi, I.; Salvesen, G.; Nagase, H. (1990). "Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts-purification and activation of the precursor and enzymic properties". Eur. J. Biochem. 194: 721–730. PMID 2269296. doi:10.1111/j.1432-1033.1990.tb19462.x.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.