EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
3.2.1.B26 | -999 |
- |
more |
kinetic constant values for soluble enzyme and for enzyme immobilized on chitosan activated with glutaraldehyde are comparable |
723982 |
3.2.1.B26 | -999 |
- |
more |
kinetic constants for transglycosylation reactions |
724763 |
3.2.1.B26 | -999 |
- |
more |
kinetic studies of the reactions of galactosylated enzyme intermediates with a range of nucleophiles |
719756 |
3.2.1.B26 | -999 |
- |
more |
KM increases with temperature: the increase is moderate at lower temperatures (from 30°C to 65°C) and more evident between 65°C and 85°C. Reactions with 4-nitrophenyl-beta-D-glucoside and 2-nitrophenyl-beta-D-glucoside show a biphasic behavior in LineweaverBurk plots, suggesting that transglycosylation reactions occur at higher substrate concentrations. Kinetic constants obtained at lower or higher substrate concentrations are calculated |
722214 |
3.2.1.B26 | 0.011 |
- |
4-methylumbelliferyl beta-D-fucopyranoside |
pH 6.5, 80°C, wild-type enzyme |
724990 |
3.2.1.B26 | 0.011 |
- |
4-methylumbelliferyl beta-D-fucoside |
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme |
724764 |
3.2.1.B26 | 0.011 |
- |
4-methylumbelliferyl beta-D-fucoside |
pH 6.5, 80°C, wild-type enzyme |
724764 |
3.2.1.B26 | 0.023 |
- |
4-methylumbelliferyl beta-D-fucopyranoside |
pH 6.5, 80°C, mutant enzyme M439C |
724990 |
3.2.1.B26 | 0.03 |
- |
2-Nitrophenyl beta-D-glucoside |
pH 6.5, 65°C, mutant enzyme E206Q |
720966 |
3.2.1.B26 | 0.03 |
- |
4-nitrophenyl beta-D-glucoside |
pH 6.5, 65°C, mutant enzyme E206Q |
720966 |