EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
3.4.24.17 | 0.9 |
- |
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2 |
wild-type enzyme form |
31010 |
3.4.24.17 | 1.4 |
- |
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2 |
truncated enzyme form |
31010 |
3.4.24.17 | 0.27 |
- |
acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly-ethylester |
- |
31012 |
3.4.24.17 | 0.025 |
- |
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2 |
- |
31015, 31017 |
3.4.24.17 | 0.05 |
- |
(7-Methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(2,4-dinitrophenyl)-Gly |
- |
31015 |
3.4.24.17 | 0.066 |
- |
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-norvaline-Trp-Met-Lys(2,4-dinitrophenyl)-NH2 |
- |
31015 |
3.4.24.17 | 0.1 |
- |
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 |
- |
31015, 31017 |
3.4.24.17 | 0.395 |
- |
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 |
pH 6.0, 25°C, catalytic domain (residues 83-247) |
717280 |
3.4.24.17 | -999 |
- |
more |
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 |
733479 |