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3.4.24.17: stromelysin 1

This is an abbreviated version!
For detailed information about stromelysin 1, go to the full flat file.

Word Map on EC 3.4.24.17

Reaction

preferential cleavage where P1', P2' and P3' are hydrophobic residues =

Synonyms

Collagen-activating protein, Collagenase activating protein, matrix metalloprotease-3, Matrix metalloproteinase 3, matrix metalloproteinase-3, matrixin, MMP-3, MMP3, Neutral proteoglycanase, Procollagenase activator, Proteoglycanase, PTR1 protein, ST1, Stromelysin, stromelysin-1, Transin

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.17 stromelysin 1

KM Value

KM Value on EC 3.4.24.17 - stromelysin 1

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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-norvaline-Trp-Met-Lys(2,4-dinitrophenyl)-NH2
-
-
0.025
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
-
-
0.05
(7-Methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(2,4-dinitrophenyl)-Gly
-
-
0.1
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2
-
-
0.27
acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly-ethylester
-
-
0.395
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5
-
pH 6.0, 25°C, catalytic domain (residues 83-247)
0.9 - 1.4
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2
additional information
additional information
thermodynamic additivity analysis using stromelysin-1 and a series of biphenyl hydroxamate ligands identified through fragment additivity, thermodynamics determined by isothermal titration calorimetry, corrected for proton transfer events, overview. Additivity arises from enthalpic effects, while interaction entropies are unfavorable, the thermodynamic behavior is masked by proton transfer
-