EC Number |
Protein Variants |
Reference |
---|
1.1.1.346 | F22Y |
the mutation causes a 2.5fold decrease in Km for 2,5-didehydro-D-gluconate whereas the value of kcat remains essentially unchanged |
440307 |
1.1.1.346 | F22Y/A272G |
substrate-binding pocket double mutant with decreased kcat value for NADPH compared to the wild type enzyme |
440311 |
1.1.1.346 | F22Y/K232G/R235G/R238H/A272G |
mutant with wild type kcat value for NADPH |
440311 |
1.1.1.346 | F22Y/K232G/R235T/R238H/A272G 420 |
mutant with decreased kcat value for NADPH compared to the wild type enzyme |
440311 |
1.1.1.346 | F22Y/K232G/R238H/A272G |
mutant with decreased kcat value for NADPH compared to the wild type enzyme |
440311 |
1.1.1.346 | 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 |
440311 |
1.1.1.346 | 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 |
657308 |
1.1.1.346 | K232G/R238H |
mutant with decreased kcat value for NADPH compared to the wild type enzyme |
440311 |
1.1.1.346 | K233G |
the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme |
440310 |
1.1.1.346 | K233H |
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity |
440310 |