Search Engineering

4.2.1.46

C187A

9.4fold decrease in turnover number for dTDP-glucose compared to wild-type value, 6fold decrease in KM-value for dTDP-glucose compared to wild-type value. 8% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme

4.2.1.46

C187S

4.1fold decrease in turnover number for dTDP-glucose compared to wild-type value, 4fold decrease in KM-value for dTDP-glucose compared to wild-type value. 5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme

4.2.1.46

D135135N/E136Q

the turnover number for dTDP-6-fluoro-6-deoxyglucose is 340fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 204fold lower than that of the wild-type enzyme

4.2.1.46

D135A

222fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.2fold increase in KM-value for dTDP-glucose compared to wild-type value. 30% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme

4.2.1.46

D135A

switch from a concerted to stepwise dehydration mechanism is due to the loss of control over the glucosyl C5–C6 bond rotation in the active site

4.2.1.46

D135A

the steady-state rate of conversion of dTDP-6-fluoro-6-deoxyglucose to dTDP-4-keto-6-deoxyglucose is identical to that of wild-type. The turnover number for dTDP-6-fluoro-6-deoxyglucose is 1.5fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 223fold lower than that of the wild-type enzyme

4.2.1.46

D135N

124fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.3fold increase in KM-value for dTDP-glucose compared to wild-type value. 9% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme

4.2.1.46

D135N

switch from a concerted to stepwise dehydration mechanism is due to the loss of control over the glucosyl C5–C6 bond rotation in the active site

4.2.1.46

D135N

the steady-state rate of conversion of dTDP-6-fluoro-6-deoxyglucose to dTDP-4-keto-6-deoxyglucose is identical to that of wild-type. The turnover number for dTDP-6-fluoro-6-deoxyglucose is 1.2fold higher than that of the wild-type enzyme, the turnover number for dTDP-glucose is 124fold lower than that of the wild-type enzyme

4.2.1.46

D135N/E136Q

204fold decrease in turnover number for dTDP-glucose compared to wild-type value, 3.2fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme