1.1.1.274: 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)
This is an abbreviated version!
For detailed information about 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), go to the full flat file.
Word Map on EC 1.1.1.274
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1.1.1.274
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2,5-diketo-d-gluconic
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corynebacterium
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2-keto-l-gulonic
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nadph-dependent
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aldo-keto
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l-ascorbic
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d-glucose
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synthesis
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citrinum
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penicillium
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activity-stained
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aldose
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cofactor-binding
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reductases
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biocatalysis
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erwinia
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error-prone
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stereo-specific
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ascorbate
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enantioselectivity
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two-phase
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pantoea
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citrea
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biotechnology
- 1.1.1.274
-
2,5-diketo-d-gluconic
- corynebacterium
-
2-keto-l-gulonic
-
nadph-dependent
-
aldo-keto
-
l-ascorbic
- d-glucose
- synthesis
- citrinum
-
penicillium
-
activity-stained
- aldose
-
cofactor-binding
- reductases
-
biocatalysis
- erwinia
-
error-prone
-
stereo-specific
- ascorbate
-
enantioselectivity
-
two-phase
-
pantoea
- citrea
- biotechnology
Reaction
Synonyms
2,5-diketo-D-gluconate reductase, 2,5-diketo-D-gluconic acid reductase, 2,5-diketo-gluconate reductase, 2,5-DKG, 2,5-DKG reductase, 2,5-DKGR, 2,5DKGR, beta-keto ester reductase, CTATCC11996_22452, Dkr, YafB, YqhE, YqhE reductase
ECTree
1.1.1.274 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)Advanced search results
results (
results (Engineering
Engineering on EC 1.1.1.274 - 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A272G
mutation increases Km and kcat compared to the wild-type enzyme
F22Y
F22Y/A272G
F22Y/K232G/R235T/R238E/A272G
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isoenzyme A, 24fold increase in kcat for NADH
F22Y/K232G/R238H/A272G
K232
isoenzyme A, designed to improve the ability to use NADH as cofactor
K232Q
isoenzyme A, designed to improve the ability to use NADH as cofactor
K232S
isoenzyme A, designed to improve the ability to use NADH as cofactor
R235G
isoenzyme A, designed to improve the ability to use NADH as cofactor
R235T
isoenzyme A, designed to improve the ability to use NADH as cofactor
R238E
isoenzyme A, designed to improve the ability to use NADH as cofactor
R238H
isoenzyme A, designed to improve the ability to use NADH as cofactor, 7fold higher activity with NADH than wild-type
additional information
F22Y
mutation reduces Km and increases kcat by 50% compared to the wild-type enzyme
F22Y/A272G
increased activity compared to the wild-type enzyme, substrate inhibition at substrate concentrations above 17.5 mM
F22Y/K232G/R238H/A272G
mutant shows a higher activity with NADH compared to the wild-type enzyme
additional information
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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
additional information
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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
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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
additional information
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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
additional information
mutagenesis of 3 amino acids in the cofactor-binding pocket, mutations lead to higher activity with NADH as cofactor
