gelatinase A;
72-kDa gelatinase;
matrix metalloproteinase 2;
type IV collagenase;
3/4 collagenase (Obsolete);
matrix metalloproteinase 5 (Obsolete);
72 kDa gelatinase type A;
collagenase IV;
collagenase type IV;
MMP 2;
type IV collagen metalloproteinase;
type IV collagenase/gelatinase;
matrix metalloproteinase 2

Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases

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

A secreted endopeptidase in peptidase family M10 (interstitial collagenase family), but possessing an additional fibronectin-like domain

1  [PMID:2994741]

Murphy G, McAlpine CG, Poll CT, Reynolds JJ.

Purification and characterization of a bone metalloproteinase that degrades gelatin and types IV and V collagen.

Biochim. Biophys. Acta. 831 (1985) 49-58.

Oryctolagus cuniculus

2  [PMID:2834383]

Collier IE, Wilhelm SM, Eisen AZ, Marmer BL, Grant GA, Seltzer JL, Kronberger A, He CS, Bauer EA, Goldberg GI.

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) 6579-87.

Homo sapiens [GN:hsa]

3  [PMID:2269296]

Okada Y, Morodomi T, Enghild JJ, Suzuki K, Yasui A, Nakanishi I, Salvesen G, Nagase H.

Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties.

Eur. J. Biochem. 194 (1990) 721-30.

Homo sapiens [GN:hsa]