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, also known as MMP2 (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 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. 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.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.