1.1.1.274	A272G	mutation increases Km and kcat compared to the wild-type enzyme	657308	
1.1.1.274	F22Y	isoenzyme A, similar kcat as wild-type	440307	
1.1.1.274	F22Y	mutation reduces Km and increases kcat by 50% compared to the wild-type enzyme	657308	
1.1.1.274	F22Y/A272G	increased activity compared to the wild-type enzyme, substrate inhibition at substrate concentrations above 17.5 mM	657308	
1.1.1.274	F22Y/A272G	isoenzyme A, reduced kcat for NADH	440311	
1.1.1.274	F22Y/K232G/R235G/R238E/A272G	isoenzyme A, increase in kcat for NADH	440311	
1.1.1.274	F22Y/K232G/R235G/R238H/A272G	isoenzyme A, increase in kcat for NADH	440311	
1.1.1.274	F22Y/K232G/R235T/R238E/A272G	isoenzyme A, 24fold increase in kcat for NADH	440311	
1.1.1.274	F22Y/K232G/R238H/A272G	isoenzyme A, increase in kcat forNADH	440311	
1.1.1.274	F22Y/K232G/R238H/A272G	mutant shows a higher activity with NADH compared to the wild-type enzyme	657308	
1.1.1.274	F22Y/S232T/R235S/R238H/A272G	isoenzyme A, increase in kcat for NADH	440311	
1.1.1.274	K232	isoenzyme A, designed to improve the ability to use NADH as cofactor	440310	
1.1.1.274	K232G/R238H	isoenzyme A, increase in kcat for NADH	440311	
1.1.1.274	K232Q	isoenzyme A, designed to improve the ability to use NADH as cofactor	440310	
1.1.1.274	K232S	isoenzyme A, designed to improve the ability to use NADH as cofactor	440310	
1.1.1.274	additional information	construction of enzyme gene knockout mutant M-AKR, that shows decreased degradation activity with testosterone, estradiol, oestrone, and methyltestosterone compared to the wild-type enzyme. Compared to the wild-type, the mutation of the endogenous 2,5DKR gene results in lower degradation of estradiol and methyltestosterone but has no effct on degradation of estrone and testosterone	-, 742259	
1.1.1.274	additional information	evaluation of the food grade expression systems NICE, Lactococcus lactis, and pSIP, Lactobacillus plantarum, for the production of 2,5-diketo-D-gluconic acid reductase from Corynebacterium glutamicum that also satisfies food safety requirements. Both systems are suitable for 2,5-DKG reductase expression, maximum production yields are obtained with Lactobacillus plantarum/pSIP609 by pH control at 6.5, overview	723915	
1.1.1.274	additional information	mutagenesis of 3 amino acids in the cofactor-binding pocket, mutations lead to higher activity with NADH as cofactor	440313	
1.1.1.274	Q192R	isoenzyme A, 2.5fold increase in kcat	440307	
1.1.1.274	R235G	isoenzyme A, designed to improve the ability to use NADH as cofactor	440310	
1.1.1.274	R235T	isoenzyme A, designed to improve the ability to use NADH as cofactor	440310	
1.1.1.274	R238E	isoenzyme A, designed to improve the ability to use NADH as cofactor	440310	
1.1.1.274	R238H	isoenzyme A, designed to improve the ability to use NADH as cofactor, 7fold higher activity with NADH than wild-type	440310