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