F22Y
the mutation causes a 2.5fold decrease in Km for 2,5-didehydro-D-gluconate whereas the value of kcat remains essentially unchanged
F22Y/A272G
substrate-binding pocket double mutant with decreased kcat value for NADPH compared to the wild type enzyme
F22Y/K232G/R235G/R238H/A272G
mutant with wild type kcat value for NADPH
F22Y/K232G/R235T/R238H/A272G 420
mutant with decreased kcat value for NADPH compared to the wild type enzyme
F22Y/K232G/R238H/A272G
mutant with decreased kcat value for NADPH compared to the wild type enzyme
F22Y/K232G/R238H/A272G
the mutant exhibits activity with NADH that is more than 2 orders of magnitude higher than that of the wild type enzyme and retains a high level of activity with NADPH
F22Y/K232G/R238H/A272G
the mutation enhances binding to NADH, while retaining to a large extent the ability to bind NADPH. The mutant is also more stable and can, therefore, be expected to exhibit greater effective activity at elevated temperatures in comparison to the wild type enzyme
K232G/R238H
mutant with decreased kcat value for NADPH compared to the wild type enzyme
K233G
the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme
K233H
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
