Protein Variants | Comment | Organism |
---|---|---|
S124A | in contrast to wild-type enzyme the mutant enzyme displays a significant deuterium kinetic isotope effect. Epimerization proceeds with a deuterium kinetic isotope effect of about 2 throughout the pH range 6.3-9.0 | Escherichia coli |
S124A/Y149F | epimerization proceeds at a turnover number that is lower by a factor of 10000000 than that of the wild-type enzyme. This is attributed to the synergistic action of Tyr149 and Ser124 in wild-type enzyme and to the absence of any internal catalysis of hydride transfer in the doubly mutated enzyme. 80% inactivation after 8 min at 50°C compared to 20% inactivation of the wild-type enzyme | Escherichia coli |
Y149F | in contrast to wild-type enzyme the mutant enzyme displays a significant deuterium kinetic isotope effect. At pH there is no significant isotope effect, but at pH 6.3, the isotope effect is 2.2 | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
GalE | - |
Escherichia coli |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
wild-type enzyme loses 20% of its activity after 8 min, mutant enzyme S124A/Y149F loses 80% of its activity after 8 min | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | 8.3 | activity of the wild-type enzyme is pH-independent in the pH-range of 5.5-9.3 | Escherichia coli |