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Results 1 - 10 of 35 > >>
EC Number
Amino acid exchange
Commentary
Reference
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
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
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
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
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
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
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
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
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
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
Results 1 - 10 of 35 > >>