EC Number |
kcat/KM Value [1/mMs-1] |
kcat/KM Value Maximum [1/mMs-1] |
Substrate |
Reference |
---|
3.2.1.B26 | -999 |
- |
more |
kinetic constants for transglycosylation reactions |
724763 |
3.2.1.B26 | -999 |
- |
more |
the efficiency (kcat/KM) increases with temperature and reaches its maximal efficiency at 65°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 | 0.0006 |
- |
4-methylumbelliferyl beta-D-galacturonate |
pH 6.5, 80°C, wild-type enzyme |
724764 |
3.2.1.B26 | 0.001 |
- |
4-methylumbelliferyl beta-D-galacturonate |
pH 6.5, 45°C, mutant enzyme E432C |
724764 |
3.2.1.B26 | 0.001 |
- |
4-methylumbelliferyl beta-D-mannoside |
pH 6.5, 45°C, mutant enzyme E432C |
724764 |
3.2.1.B26 | 0.001 |
- |
4-nitrophenyl beta-D-mannoside |
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C |
724764 |
3.2.1.B26 | 0.0013 |
- |
4-methylumbelliferyl beta-D-galacturonate |
pH 6.5, 45°C, mutant enzyme W433C |
724764 |
3.2.1.B26 | 0.002 |
- |
4-methylumbelliferyl beta-D-xyloside |
pH 6.5, 45°C, mutant enzyme E432C |
724764 |
3.2.1.B26 | 0.002 |
- |
4-nitrophenyl beta-D-xyloside |
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C |
724764 |
3.2.1.B26 | 0.0022 |
- |
4-methylumbelliferyl beta-D-xyloside |
pH 6.5, 80°C, mutant enzyme E432C |
724764 |