Ile-Ala-Gly-Gln
Reaction: Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-GlyIle-Ala-Gly-Gln
Other name(s): 72-kDa gelatinase; matrix metalloproteinase 2; type IV collagenase (ambiguous); 3/4 collagenase (obsolete); matrix metalloproteinase 5 (obsolete); 72 kDa gelatinase type A; collagenase IV (ambiguous); collagenase type IV (ambiguous); MMP 2; type IV collagen metalloproteinase (ambiguous); type IV collagenase/gelatinase (ambiguous)
Comments: A secreted endopeptidase In peptidase family M10 (interstitial collagenase family), but possessing an additional fibronectin-like domain
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 146480-35-5
References:
1. Murphy, G., McAlpine, C.G., Poll, C.T. and Reynolds, J.J. Purification and characterization of a bone metalloproteinase that degrades gelatin and types IV and V collagen. Biochim. Biophys. Acta 831 (1985) 49-58. [PMID: 2994741]
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. and Goldberg, G.I. H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. J. Biol. Chem. 263 (1988) 6579-6587. [PMID: 2834383]
3. Okada, Y., Morodomi, T., Enghild, J.J., Suzuki, K., Yasui, A., Nakanishi, I., Salvesen, G. and Nagase, H. Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts-purification and activation of the precursor and enzymic properties. Eur. J. Biochem. 194 (1990) 721-730. [PMID: 2269296]