EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
2.5.1.18 | -999 |
- |
more |
- |
637902, 637906, 637914, 637920, 637924, 637931, 672693, 674220 |
2.5.1.18 | -999 |
- |
more |
a sequential steady-state kinetic mechanism |
674395 |
2.5.1.18 | -999 |
- |
more |
biphasic kinetics of enzyme from healthy and muscle with experimental trichinellosis in presence or absence of albendazole, overview |
676292 |
2.5.1.18 | -999 |
- |
more |
Cu2+ effects on Km, overview |
673034 |
2.5.1.18 | -999 |
- |
more |
GST5118 kinetic mechanism, overview |
722794 |
2.5.1.18 | -999 |
- |
more |
isothermal titration calorimetry reveals high-affinity binding for GSTF2 and GSTF3, which is enhanced in the presence of glutathione and by the other heterocyclic ligands, and allosteric enhancement in glutathione-conjugating activity |
721531 |
2.5.1.18 | -999 |
- |
more |
kinetic analysis of wild-type and mutant enzymes, overview |
702461 |
2.5.1.18 | -999 |
- |
more |
kinetic analysis, overview |
702461 |
2.5.1.18 | -999 |
- |
more |
kinetic analysis, overview. GSTM2-2 does not follow a rapid equilibrium Michaelis-Menten mechanism. However, the low catalytic activity of the GSTM2-2 isoenzyme and its high affinity for brostallicin prevent an accurate kinetic study |
702366 |
2.5.1.18 | -999 |
- |
more |
kinetics |
703303 |