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3.4.24.23: matrilysin

This is an abbreviated version!
For detailed information about matrilysin, go to the full flat file.

Word Map on EC 3.4.24.23

Reaction

Cleavage of Ala14-/-Leu and Tyr16-/-Leu in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha2(I) > alpha1(I) =

Synonyms

cyclic matrix metalloproteinase, human matrix metalloproteinase 7, matrilysin, matrilysin 1, matrilysin-1, Matrin, matrix metallopeptidase 7, matrix metalloprotease-7, Matrix metalloproteinase 7, Matrix metalloproteinase pump 1, Matrix metalloproteinase-7, matrix-metalloproteinase-7, metalloproteinase-7, MMP, MMP 7, MMP-7, MMP7, More, Proteinase, metallo-, pump-1, Proteinase, PUMP-1, PUMP, PUMP-1, Pump-1 protease, Putative (or punctuated) metalloproteinase-1, Putative metalloproteinase, Uterine metalloendopeptidase, Uterine metalloproteinase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.23 matrilysin

pH Range

pH Range on EC 3.4.24.23 - matrilysin

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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
-
4.5 - 8.5
-
4.5: about 40% of activity maximum, 8.5: about 65% of activity maximum, 2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg
4.5 - 9.5
-
-
5 - 9
-
maximal activity range of wild-type enzyme, and mutants Y193F and Y216F
5.5 - 8.8
-
5.5: about 30% of activity maximum, 8.8: about 40% of activity maximum