Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-naphthoquinone + NADPH
? + NADP+
-
-
-
-
?
2,5-didehydro-D-gluconate + NADH
2-keto-L-gulonate + NAD+
2,5-didehydro-D-gluconate + NADPH
2-keto-L-gulonate + NADP+
2,5-didehydro-D-gluconate + NADPH
2-oxo-L-gulonic acid + NADP+
2,5-didehydro-D-gluconate + NADPH + H+
2-dehydro-D-gluconate + NADP+
-
-
-
?
2,5-diketo-D-gluconate + NADPH
? + NADP+
-
-
-
-
?
2-carboxybenzaldehyde + NADPH
2-hydroxybenzoate + NADP+
-
-
-
-
?
2-dehydro-D-gulonate + NADP+
2,5-didehydro-D-gluconate + NADPH + H+
3-nitrobenzaldehyde + NADPH
3-nitrobenzyl alcohol + NADP+
-
-
-
-
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
-
-
-
?
5-keto-D-fructose + NADPH
L-sorbose + NADP+
benzaldehyde + NADPH
benzyl alcohol + NADP+
-
-
-
-
?
D-glucuronic acid + NADPH
? + NADP+
-
-
-
-
?
D-xylose + NADPH
? + NADP+
-
-
-
-
?
dihydroxyacetone + NADPH
glycerol + NADP+
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
?
ethyl 2-ethylacetoacetate + NADPH
ethyl (2R)-ethyl-(3S)-hydroxybutanoate + NADP+
-
stereospecific reaction
-
-
?
ethyl 2-methylacetoacetate + NADPH
ethyl (2R)-methyl-(3S)-hydroxybutanoate + NADP+
-
stereospecific reaction
-
-
?
ethyl 2-methylacetoacetate + NADPH + H+
ethyl (2R)-methyl-(3S)-hydroxybutanoate + NADP+
ethyl acetoacetate + NADPH
ethyl (3S)-hydroxybutanoate + NADP+
-
stereospecific reaction
-
-
?
ethyl-(2R)-allylacetoacetate + NADPH
?
-
250% of activity with ethyl-2-methylacetoacetate
-
-
?
ethyl-(2R)-ethylacetoacetate + NADPH
ethyl-(2R)-ethyl-(3S)-hydroxybutanoate + NADP+
ethylacetoacetate + NADPH
ethyl-(3S)-hydroxybutanoate + NADP+
methylglyoxal + NADPH
? + NADP+
-
-
-
-
?
phenylglyoxal + NADPH
? + NADP+
-
-
-
-
?
additional information
?
-
2,5-didehydro-D-gluconate + NADH
2-keto-L-gulonate + NAD+
-
-
-
-
?
2,5-didehydro-D-gluconate + NADH
2-keto-L-gulonate + NAD+
-
-
-
?
2,5-didehydro-D-gluconate + NADH
2-keto-L-gulonate + NAD+
-
170fold lower reduction rate with NADH compared to NADPH
-
?
2,5-didehydro-D-gluconate + NADH
2-keto-L-gulonate + NAD+
-
170fold lower reduction rate with NADH compared to NADPH
-
?
2,5-didehydro-D-gluconate + NADPH
2-keto-L-gulonate + NADP+
-
-
-
?
2,5-didehydro-D-gluconate + NADPH
2-keto-L-gulonate + NADP+
-
stereospecific reduction to 2-keto-L-gulonate, no activity with D-fructose, L-sorbose, 5-keto-D-gluconate, 2-keto-L-gulonate, 2-keto-D-gluconate, pyruvate or hydroxypyruvate
-
r
2,5-didehydro-D-gluconate + NADPH
2-keto-L-gulonate + NADP+
-
stereospecific reduction to 2-keto-L-gulonate, no activity with D-fructose, L-sorbose, 5-keto-D-gluconate, 2-keto-L-gulonate, 2-keto-D-gluconate, pyruvate or hydroxypyruvate
-
r
2,5-didehydro-D-gluconate + NADPH
2-keto-L-gulonate + NADP+
-
-
-
?
2,5-didehydro-D-gluconate + NADPH
2-keto-L-gulonate + NADP+
-
-
-
?
2,5-didehydro-D-gluconate + NADPH
2-keto-L-gulonate + NADP+
both isoenzymes A and B are specific for NADPH
-
?
2,5-didehydro-D-gluconate + NADPH
2-keto-L-gulonate + NADP+
-
-
-
?
2,5-didehydro-D-gluconate + NADPH
2-oxo-L-gulonic acid + NADP+
step in the biosynthesis of L-ascorbic acid
-
-
?
2,5-didehydro-D-gluconate + NADPH
2-oxo-L-gulonic acid + NADP+
i.e. 2,5-diketo-D-gluconic acid or 2,5-DKG, stereospecific reaction
i.e. 2-keto-L-gulonic acid or 2-KLG, product is a precursor for L-ascorbic acid
-
?
2-dehydro-D-gulonate + NADP+
2,5-didehydro-D-gluconate + NADPH + H+
-
-
-
-
?
2-dehydro-D-gulonate + NADP+
2,5-didehydro-D-gluconate + NADPH + H+
-
-
-
-
?
5-keto-D-fructose + NADPH
L-sorbose + NADP+
-
-
-
?
5-keto-D-fructose + NADPH
L-sorbose + NADP+
-
isoenzymes I and II
-
?
5-keto-D-fructose + NADPH
L-sorbose + NADP+
-
-
-
?
5-keto-D-fructose + NADPH
L-sorbose + NADP+
-
isoenzymes I and II
-
?
dihydroxyacetone + NADPH
glycerol + NADP+
-
-
-
?
dihydroxyacetone + NADPH
glycerol + NADP+
-
-
-
-
?
dihydroxyacetone + NADPH
glycerol + NADP+
-
-
-
-
?
dihydroxyacetone + NADPH
glycerol + NADP+
-
-
-
?
ethyl 2-methylacetoacetate + NADPH + H+
ethyl (2R)-methyl-(3S)-hydroxybutanoate + NADP+
-
7% activity with NADH
-
?
ethyl 2-methylacetoacetate + NADPH + H+
ethyl (2R)-methyl-(3S)-hydroxybutanoate + NADP+
-
7% activity with NADH
-
?
ethyl-(2R)-ethylacetoacetate + NADPH
ethyl-(2R)-ethyl-(3S)-hydroxybutanoate + NADP+
-
120% of activity with ethyl-2-methylacetoacetate
-
?
ethyl-(2R)-ethylacetoacetate + NADPH
ethyl-(2R)-ethyl-(3S)-hydroxybutanoate + NADP+
-
120% of activity with ethyl-2-methylacetoacetate
-
?
ethylacetoacetate + NADPH
ethyl-(3S)-hydroxybutanoate + NADP+
-
53% of activity with ethyl-2-methylacetoacetate
-
?
ethylacetoacetate + NADPH
ethyl-(3S)-hydroxybutanoate + NADP+
-
53% of activity with ethyl-2-methylacetoacetate
-
?
additional information
?
-
-
the enzyme catalyzes degradation of estradiol, estrone, testosterone, and methyltestosterone, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes degradation of estradiol, estrone, testosterone, and methyltestosterone, overview
-
-
?
additional information
?
-
isozyme A is more stable than isozyme B but less active
-
-
?
additional information
?
-
-
substrate specificity, no activity with ethyl propionyl acetate and ethyl butyryl acetate
-
-
?
additional information
?
-
-
substrate specificity, no activity with ethyl propionyl acetate and ethyl butyryl acetate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,5-didehydro-D-gluconate + NADPH
2-oxo-L-gulonic acid + NADP+
step in the biosynthesis of L-ascorbic acid
-
-
?
2,5-didehydro-D-gluconate + NADPH + H+
2-dehydro-D-gluconate + NADP+
-
-
-
?
2-dehydro-D-gulonate + NADP+
2,5-didehydro-D-gluconate + NADPH + H+
ethyl 2-ethylacetoacetate + NADPH
ethyl (2R)-ethyl-(3S)-hydroxybutanoate + NADP+
-
stereospecific reaction
-
-
?
ethyl 2-methylacetoacetate + NADPH
ethyl (2R)-methyl-(3S)-hydroxybutanoate + NADP+
-
stereospecific reaction
-
-
?
ethyl acetoacetate + NADPH
ethyl (3S)-hydroxybutanoate + NADP+
-
stereospecific reaction
-
-
?
additional information
?
-
2-dehydro-D-gulonate + NADP+
2,5-didehydro-D-gluconate + NADPH + H+
-
-
-
-
?
2-dehydro-D-gulonate + NADP+
2,5-didehydro-D-gluconate + NADPH + H+
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes degradation of estradiol, estrone, testosterone, and methyltestosterone, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes degradation of estradiol, estrone, testosterone, and methyltestosterone, overview
-
-
?
additional information
?
-
-
substrate specificity, no activity with ethyl propionyl acetate and ethyl butyryl acetate
-
-
?
additional information
?
-
-
substrate specificity, no activity with ethyl propionyl acetate and ethyl butyryl acetate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0123 - 150
2,5-didehydro-D-gluconate
155
5-keto-D-fructose
-
-
3.1
ethyl 2-methylacetoacetate
-
pH 7.0, 30°C, with a cofactor level 20fold higher than the Km value
3.1
ethyl-2-methylacetoacetate
-
-
2.05 - 2.46
methylglyoxal
additional information
additional information
-
-
-
0.0123
2,5-didehydro-D-gluconate
-
isoenzyme A, F22Y mutant enzyme
0.0312
2,5-didehydro-D-gluconate
-
isoenzyme A, wild-type
0.39
2,5-didehydro-D-gluconate
-
F22Y/K232G/R235T/R238H/A272G isoenzyme A mutant
1.8
2,5-didehydro-D-gluconate
-
isoenzyme I
7.2
2,5-didehydro-D-gluconate
-
F22Y/A272G isoenzyme A mutant
8.7
2,5-didehydro-D-gluconate
-
F22Y/K232G/R235T/R238H/A272G isoenzyme A mutant
9.1
2,5-didehydro-D-gluconate
-
F22Y/K232G/R238H/A272G isoenzyme A mutant
13
2,5-didehydro-D-gluconate
-
K232G/R238H isoenzyme A mutant
13
2,5-didehydro-D-gluconate
-
F22Y/K232G/R235G/R238E/A272G isoenzyme A mutant
13.5
2,5-didehydro-D-gluconate
-
isoenzyme II
26
2,5-didehydro-D-gluconate
-
-
27
2,5-didehydro-D-gluconate
-
F22Y/S232T/R235S/R238H/A272G isoenzyme A mutant
30
2,5-didehydro-D-gluconate
-
F22Y/A272G isoenzyme A mutant
32
2,5-didehydro-D-gluconate
-
F22Y/K232G/R238H/A272G isoenzyme A mutant
32
2,5-didehydro-D-gluconate
-
F22Y/K232G/R235G/R238H/A272G isoenzyme A mutant
43
2,5-didehydro-D-gluconate
-
F22Y/K232G/R235G/R238H/A272G isoenzyme A mutant
110
2,5-didehydro-D-gluconate
-
K232G/R238H isoenzyme A mutant
130
2,5-didehydro-D-gluconate
-
isoenzyme A, wild-type
150
2,5-didehydro-D-gluconate
-
F22Y/K232G/R235T/R238E/A272G isoenzyme A mutant
2.05
methylglyoxal
-
YqhE
2.46
methylglyoxal
-
YafB
0.66
NADH
-
K232G/R238H isoenzyme A mutant
1.2
NADH
-
F22Y/K232G/R238H/A272G isoenzyme A mutant
1.4
NADH
-
isoenzyme A, wild-type
2
NADH
isoenzyme A, K232G mutant
2.1
NADH
isoenzyme A, R238H mutant
2.4
NADH
-
F22Y/A272G isoenzyme A mutant
2.6
NADH
isoenzyme A, wild-type
2.7
NADH
-
F22Y/K232G/R235G/R238H/A272G isoenzyme A mutant
2.8
NADH
isoenzyme A, K232S mutant
3.4
NADH
-
F22Y/K232G/R235G/R238E/A272G isoenzyme A mutant
3.9
NADH
isoenzyme A, K232M mutant
3.9
NADH
isoenzyme A, K232Q mutant
3.9
NADH
-
F22Y/S233T/R235S/R238H/A272G isoenzyme A mutant
5.2
NADH
-
F22Y/K232G/R235T/R238E/A272G isoenzyme A mutant
8.4
NADH
isoenzyme A, R235G mutant
8.4
NADH
isoenzyme A, R238E mutant
8.8
NADH
isoenzyme A, R235T mutant
0.01
NADPH
-
-
0.039
NADPH
-
F22Y/A272G isoenzyme A mutant
0.055
NADPH
-
F22Y/S233T/R235S/R238H/A272G isoenzyme A mutant
0.058
NADPH
-
F22Y/K232G/R238H/A272G isoenzyme A mutant
0.071
NADPH
-
F22Y/K232G/R235T/R238H/A272G isoenzyme A mutant
0.13
NADPH
-
K232G/R238H isoenzyme A mutant
0.15
NADPH
-
F22Y/K232G/R235G/R238H/A272G isoenzyme A mutant
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0153
-
YafB, 10 mM D-glucuronic acid as substrate
0.0247
-
YqhE, 10 mM D-glucuronic acid as substrate
0.0401
-
YafB, 1 mM 2,5-diketo-D-gluconate as substrate
0.0424
-
YafB, 0.1 mM 1,2-naphthoquinone as substrate
0.0519
-
YqhE, 1 mM 2,5-diketo-D-gluconate as substrate
0.0949
-
YqhE, 10 mM D-xylose as substrate
0.127
-
YqhE, 0.1 mM 1,2-naphthoquinone as substrate
1.36
-
YafB, 1 mM DL-glyceraldehyde as substrate
10.3
-
YqhE, 1 mM 4-nitrobenzaldehyde as substrate
14.9
-
YafB, 1 mM methylglyoxal as substrate
2.21
-
YqhE, 1 mM DL-glyceraldehyde as substrate
2.23
-
YafB, 1 mM 3-nitrobenzaldehyde as substrate
2.5
-
YqhE, 1 mM 3-nitrobenzaldehyde as substrate
2.79
-
YafB, 1 mM benzaldehyde as substrate
21
-
YqhE, 1 mM methylglyoxal as substrate
3.88
-
YqhE, 1 mM benzaldehyde as substrate
39.1
-
YafB, 1 mM phenylglyoxal as substrate
6.53
-
YafB, 1 mM 4-nitrobenzaldehyde as substrate
64.4
-
YqhE, 1 mM phenylglyoxal as substrate
0.01
-
YafB, 1 mM 2-carboxybenzaldehyde as substrate
0.01
-
YafB, 10 mM D-xylose as substrate
0.01
-
YqhE, 1 mM 2-carboxybenzaldehyde as substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
physiological function
2,5-diketo-D-gluconic acid reductase catalyses the reduction of 2,5-diketo-D-gluconic acid to 2-keto-L-gulonic acid, a direct precursor (lactone) of L-ascorbic acid (vitamin C). This reaction is an essential step in the biocatalytic production of the food supplement vitamin C from D-glucose or D-gluconic acid
evolution
-
the enzyme belongs to the AKR superfamily, monomeric (alpha/beta) 8-barrel proteins which bind NAD(P)(H) to metabolize an array of substrates
evolution
-
the enzyme belongs to the AKR superfamily, monomeric (alpha/beta) 8-barrel proteins which bind NAD(P)(H) to metabolize an array of substrates
-
malfunction
-
compared to the wild-type, the knockout 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. Cell growth on ethanol, oestrone, estradiol, testosterone or methyltestosterone is reduced in the mutant strain compared to the wild-type
malfunction
-
compared to the wild-type, the knockout 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. Cell growth on ethanol, oestrone, estradiol, testosterone or methyltestosterone is reduced in the mutant strain compared to the wild-type
-
additional information
-
three consensus sequences of the AKR superfamily are found as GxxxxDxAxxY, LxxxGxxxPxxGxG and LxxxxxxxxxDxxxxH. GxxxxDxAxxY is the active site, LxxxGxxxPxxGxG is the cofactor-binding site for NAD(P)(H), and LxxxxxxxxxDxxxxH is required for supporting the 3D structure
additional information
-
three consensus sequences of the AKR superfamily are found as GxxxxDxAxxY, LxxxGxxxPxxGxG and LxxxxxxxxxDxxxxH. GxxxxDxAxxY is the active site, LxxxGxxxPxxGxG is the cofactor-binding site for NAD(P)(H), and LxxxxxxxxxDxxxxH is required for supporting the 3D structure
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A272G
mutation increases Km and kcat compared to the wild-type enzyme
F22Y/K232G/R235G/R238E/A272G
-
isoenzyme A, increase in kcat for NADH
F22Y/K232G/R235G/R238H/A272G
-
isoenzyme A, increase in kcat for NADH
F22Y/K232G/R235T/R238E/A272G
-
isoenzyme A, 24fold increase in kcat for NADH
F22Y/S232T/R235S/R238H/A272G
-
isoenzyme A, increase in kcat for NADH
K232
isoenzyme A, designed to improve the ability to use NADH as cofactor
K232G/R238H
-
isoenzyme A, increase in kcat for NADH
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
Q192R
-
isoenzyme A, 2.5fold increase in kcat
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
F22Y
-
isoenzyme A, similar kcat as wild-type
F22Y
mutation reduces Km and increases kcat by 50% compared to the wild-type enzyme
F22Y/A272G
-
isoenzyme A, reduced kcat for NADH
F22Y/A272G
increased activity compared to the wild-type enzyme, substrate inhibition at substrate concentrations above 17.5 mM
F22Y/K232G/R238H/A272G
-
isoenzyme A, increase in kcat forNADH
F22Y/K232G/R238H/A272G
mutant shows a higher activity with NADH compared to the wild-type enzyme
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
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
-
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Sonoyama, T.; Kobayashi, K.
Purification and properties of two 2,5-diketo-D-gluconate reductases from a mutant strain derived from Corynebacterium sp
J. Ferment. Technol.
65
311-317
1987
Corynebacterium sp.
-
brenda
Miller, J.V.; Estell, D.A.; Lazarus, R.A.
Purification and characterization of 2,5-diketo-D-gluconate reductase from Corynebacterium sp
J. Biol. Chem.
262
9016-9020
1987
Corynebacterium sp.
brenda
Khurana, S.; Powers, D.B.; Anderson, S.; Blaber, M.
Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1 A resolution
Proc. Natl. Acad. Sci. USA
95
6768-6773
1998
Corynebacterium sp.
brenda
Yum, D.Y.; Lee, B.Y.; Pan, J.G.
Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-gluconate reductases in Escherichia coli
Appl. Environ. Microbiol.
65
3341-3346
1999
Escherichia coli (P30863)
brenda
Khurana, S.; Sanli, G.; Powers, D.B.; Anderson, S.; Blaber, M.
Molecular modeling of substrate binding in wild-type and mutant Corynebacteria 2,5-diketo-D-gluconate reductases
Proteins
39
68-75
2000
Corynebacterium sp.
brenda
Ji, A.; Gao, P.
Substrate selectivity of Gluconobacter oxydans for production of 2,5-diketo-D-gluconic acid and synthesis of 2-keto-L-gulonic acid in a multienzyme system
Appl. Biochem. Biotechnol.
94
213-223
2001
Corynebacterium sp.
brenda
Sanli, G.; Blaber, M.
Structural assembly of the active site in an aldo-keto reductase by NADPH cofactor
J. Mol. Biol.
309
1209-1218
2001
Corynebacterium sp. (P06632)
brenda
Banta, S.; Swanson, B.A.; Wu, S.; Jarnagin, A.; Anderson, S.
Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase A
Protein Eng.
15
131-140
2002
Corynebacterium sp. (P06632)
brenda
Banta, S.; Swanson, B.A.; Wu, S.; Jarnagin, A.; Anderson, S.
Optimizing an artificial metabolic pathway: engineering the cofactor specificity of Corynebacterium 2,5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis
Biochemistry
41
6226-6236
2002
Corynebacterium sp.
brenda
Habrych, M.; Rodriguez, S.; Stewart, J.D.
Purification and identification of an Escherichia coli beta-keto ester reductase as 2,5-diketo-D-gluconate reductase YqhE
Biotechnol. Prog.
18
257-261
2002
Escherichia coli
brenda
Banta, S.; Anderson, S.
Verification of a novel NADH-binding motif: combinatorial mutagenesis of three amino acids in the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase
J. Mol. Evol.
55
623-631
2002
Corynebacterium sp. (P06632)
brenda
Sanli, G.; Banta, S.; Anderson, S.; Blaber, M.
Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase
Protein Sci.
13
504-512
2004
Corynebacterium sp. (P06632)
brenda
Ko, J.; Kim, I.; Yoo, S.; Min, B.; Kim, K.; Park, C.
Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases
J. Bacteriol.
187
5782-5789
2005
Escherichia coli
brenda
Kaswurm, V.; Nguyen, T.T.; Maischberger, T.; Kulbe, K.D.; Michlmayr, H.
Evaluation of the food grade expression systems NICE and pSIP for the production of 2,5-diketo-D-gluconic acid reductase from Corynebacterium glutamicum
AMB Express
3
7-7
2013
Corynebacterium glutamicum (H9CWC0), Corynebacterium glutamicum
brenda
Kaswurm, V.; van Hecke, W.; Kulbe, K.; Ludwig, R.
Engineering of a bi-enzymatic reaction for efficient production of the ascorbic acid precursor 2-keto-L-gulonic acid
Biochem. Eng. J.
79
104-111
2013
Corynebacterium glutamicum (H9CWC0)
-
brenda
Chen, Y.; Ji, W.; Zhang, H.; Zhang, X.; Yu, Y.
Cloning, expression and characterization of a putative 2,5-diketo-D-gluconic acid reductase in Comamonas testosteroni
Chem. Biol. Interact.
234
229-235
2015
Comamonas testosteroni, Comamonas testosteroni ATCC 11996
brenda