Stromelysin 2
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.24 Metalloendopeptidases > 3.4.24.22 stromelysin 2
Matrilysin is a 19-kDa zinc metalloendopeptidase found in rat uterus, the smallest member of peptidase family M10 (interstitial collagenase family). Its specificity resembles stromelysin but it is more active on azocoll; it cleaves Ala14-/-Leu and Tyr16-/-Leu in the insulin B chain, has no action on collagen types I, II, IV and V, and cleaves gelatin chain alpha2(I) more than alpha1(I). In uterus and epithelia it remodels matrix at tissue-remodeling sites. It is the minimal domain form of MMPs lacking the hemopexin domain.
Matrilysin is a 19-kDa zinc metalloendopeptidase found in rat uterus, the smallest member of peptidase family M10 (interstitial collagenase family). Its specificity resembles stromelysin but it is more active on azocoll; it cleaves Ala14-/-Leu and Tyr16-/-Leu in the insulin B chain, has no action on collagen types I, II, IV and V, and cleaves gelatin chain alpha2(I) more than alpha1(I). In uterus and epithelia it remodels matrix at tissue-remodeling sites. It is the minimal domain form of MMPs lacking the hemopexin domain.
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