EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   3.4.24.80 | -999 |
- |
more |
increase in substrate triple-helical thermal stability is not detrimental to enzyme binding of substrate |
667581 |
| 3.4.24.80 | -999 |
- |
more |
Michaelis-Menten kinetics |
755435 |
| 3.4.24.80 | -999 |
- |
more |
steady-state kinetics and thermodynamics over a wide range of temperatures and pressures, stopped-flow fluorescence technique |
753019 |
| 3.4.24.80 | 0.000034 |
- |
type I collagen chain alpha-1 |
at 37°C |
681426 |
| 3.4.24.80 | 0.000035 |
- |
type I collagen chain alpha-2 |
at 37°C |
681426 |
| 3.4.24.80 | 0.00025 |
- |
collagen type I alpha-2 chain |
1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C |
717876 |
| 3.4.24.80 | 0.0003 |
- |
collagen I alpha-1 chain |
pH not specified in the publication, 37°C, MMP-1: 1-protonated |
717876 |
| 3.4.24.80 | 0.0006 |
- |
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 |
pH 7.0, 10°C, recombinant enzyme |
753019 |
| 3.4.24.80 | 0.00065 |
- |
collagen I alpha-2 chain |
pH not specified in the publication, 37°C, MMP-1: 3-protonated |
717876 |
| 3.4.24.80 | 0.00077 |
- |
collagen I alpha-1 chain |
pH not specified in the publication, 37°C, MMP-1: 2-protonated |
717876 |
