1.1.1.346: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)
This is an abbreviated version!
For detailed information about 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), go to the full flat file.
Reaction
Synonyms
2,5-diketo-D-gluconate reductase, 2,5-diketo-D-gluconate reductase I, 2,5-diketo-D-gluconate reductase II, 2,5-diketo-D-gluconate-reductase, 2,5-diketo-D-gluconic acid reductase, 2,5-diketo-D-gluconic acid reductase A, 2,5-DKG reductase, 2,5-DKGR A, 2,5-DKGR B, 2,5-DKGRA, 2,5DKGR, 25DKG reductase, 25DKGR-A, 2KR, AKR5C, CTATCC11996_22452, dkgA, dkgB, Dkr, YqhE, YqhE reductase
ECTree
1.1.1.346 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)Advanced search results
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results (Engineering
Engineering on EC 1.1.1.346 - 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F22Y
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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
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substrate-binding pocket double mutant with decreased kcat value for NADPH compared to the wild type enzyme
F22Y/K232G/R235G/R238H/A272G
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mutant with wild type kcat value for NADPH
F22Y/K232G/R235T/R238H/A272G 420
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mutant with decreased kcat value for NADPH compared to the wild type enzyme
F22Y/K232G/R238H/A272G
K232G/R238H
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mutant with decreased kcat value for NADPH compared to the wild type enzyme
K233G
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the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme
K233H
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the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
K233M
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the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme
K233Q
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the mutant shows wild type NADPH activity and increased NADH activity
K233R
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the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
K233S
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the mutant shows wild type NADPH activity and increased NADH activity compared to the wild type enzyme
Q192R
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the mutation primarily affects the kcat parameter toward the 2,5-didehydro-D-gluconate substrate, increasing its value approximately 2.5fold, whereas Km is relatively unaffected, or increases slightly
R235D
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the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
R235E
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the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
R235G
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the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme
R235T
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the mutant shows wild type NADPH activity and increased NADH activity
R235Y
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the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity
R238E
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the mutant shows no activity with NADPH and increased NADH activity compared to the wild type enzyme
R238G
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the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity
R238H
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the mutant shows wild type NADPH activity and increased NADH activity
R238Q
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the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity
R238Y
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the mutant shows reduced NADPH activity and increased NADH activity ompared to the wild type enzyme
V234M/R235C
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the mutant shows wild type NADPH activity and no NADH activity
V234S
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the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
additional information
F22Y/K232G/R238H/A272G
-
mutant with decreased kcat value for NADPH compared to the wild type enzyme
F22Y/K232G/R238H/A272G
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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
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
-
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
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establishment of an efficient process for 2,5-DKG reductase production that also satisfies food safety requirements. Food grade variants of the Lactobacillales based expression systems pSIP (Lactobacillus plantarum) and NICE (Lactococcus lactis) are evaluated with regard to their effictiveness to produce 2,5-DKG reductase from Corynebacterium glutamicum, overview. Lactobacillus plantarum/pSIP609 is an interesting alternative to Escherichia coli expression systems for industrial 2,5-DKG reductase production. Highest production levels of 2,5-DKG reductase are obtained with the system Lactobacillus plantarum/pSIP609, resulting in 104 U/l without pH regulation and 262 U/l with pH control at pH 6.5
additional information
-
establishment of an efficient process for 2,5-DKG reductase production that also satisfies food safety requirements. Food grade variants of the Lactobacillales based expression systems pSIP (Lactobacillus plantarum) and NICE (Lactococcus lactis) are evaluated with regard to their effictiveness to produce 2,5-DKG reductase from Corynebacterium glutamicum, overview. Lactobacillus plantarum/pSIP609 is an interesting alternative to Escherichia coli expression systems for industrial 2,5-DKG reductase production. Highest production levels of 2,5-DKG reductase are obtained with the system Lactobacillus plantarum/pSIP609, resulting in 104 U/l without pH regulation and 262 U/l with pH control at pH 6.5
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