HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.1.1.274 - 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)
for references in articles please use BRENDA:EC1.1.1.274Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.274 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)IUBMB Comments
The enzyme is involved in the catabolism of 2,5-didehydrogluconate. cf. EC 1.1.1.346, 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming).
Specify your search results
Word Map
- 1.1.1.274
-
2,5-diketo-d-gluconic
-
2-keto-l-gulonic
- corynebacterium
-
nadph-dependent
-
aldo-keto
-
l-ascorbic
- d-glucose
-
cofactor-binding
- synthesis
- citrinum
- reductases
- aldose
-
penicillium
-
activity-stained
- ascorbate
-
stereo-specific
- erwinia
-
error-prone
-
enantioselectivity
-
biocatalysis
-
pantoea
- citrea
-
two-phase
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
2,5-dkg reductase, 2,5-dkg, 2,5-dkgr, 2,5-diketo-d-gluconate reductase, beta-keto ester reductase, yqhe reductase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,5-diketo-D-gluconate reductase
2,5-diketo-D-gluconic acid reductase
2,5-DKG
2,5DKGR
beta-keto ester reductase
CTATCC11996_22452
YqhE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
reaction mechanism
-
2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
catalytic mechanism
-
2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
enzyme also possesses beta-keto ester reductase activity
-
2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
reaction mechanism of wild-type and F22Y/K232G/R238H/A272G mutant enzyme
2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
enzyme also possesses beta-keto ester reductase activity
-
2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
2-dehydro-D-gluconate:NADP+ 2-oxidoreductase (2-dehydro-D-gluconate-forming)
The enzyme is involved in the catabolism of 2,5-didehydrogluconate. cf. EC 1.1.1.346, 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
95725-95-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,5-didehydro-D-gluconate + NADPH + H+
2-dehydro-D-gluconate + 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 acetoacetate + NADPH
ethyl (3S)-hydroxybutanoate + NADP+
-
stereospecific reaction
-
?
ethyl-(2R)-allylacetoacetate + NADPH
?
-
250% of activity with ethyl-2-methylacetoacetate
-
?
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+
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+
-
isoenzymes I and II
-
?
5-keto-D-fructose + NADPH
L-sorbose + NADP+
-
isoenzymes I and II
-
?
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.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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+
-
-
-
?
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
-
-
?
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.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
cofactor binding structure of wild-type and F22Y/K232G/R238H/A272G mutant enzyme, involved Lys232, Ala272, and Arg238
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,5-didehydro-D-gluconate
substrate inhibition of isozyme B, not of isozyme A, at high concentrations
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
ethyl 2-methylacetoacetate
-
pH 7.0, 30°C, with a cofactor level 20fold higher than the Km value
0.39
2,5-didehydro-D-gluconate
-
F22Y/K232G/R235T/R238H/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
-
F22Y/K232G/R235G/R238E/A272G isoenzyme A mutant
27
2,5-didehydro-D-gluconate
-
F22Y/S232T/R235S/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
150
2,5-didehydro-D-gluconate
-
F22Y/K232G/R235T/R238E/A272G isoenzyme A mutant
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
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
additional information
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
Show AA Sequence and Transmembrane Helices (2957 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
34000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
-
x * 39400, about, sequence calculation, x * 41600, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 39400, about, sequence calculation, x * 41600, recombinant His-tagged enzyme, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
10 mg/ml purified recombinant F22Y/K232G/R238H/A272G mutant enzyme in complex with NADH in 25 mM Tris-HCl, pH 7.5, 1 mM NADH, hanging drop vapour diffusion method, room temperature, equal volumes, 0.005 ml each, of protein and crystallization solution against 1 ml reservoir crystallization solution containing 1.5 M lithium sulfate, 0.1 M Na-HEPES, pH 7.5, 7-10 days, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacment, molecular modeling of substrate and cofactor binding
isoenzyme A, hanging drop-vapour diffusion, 1.9 A resolution of apo enzyme
isoenzyme A, hanging-drop vapour diffusion, X-ray structure of complex with NADPH, 2.1 A resolution
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
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.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
thermodynamic stability study of wild-type and F22Y/K232G/R238H/A272G mutant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme, 400 mM potassium phoshate buffer, pH 7.0, several weeks without appreciable loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-Sepharose, Matrix Red-A, Sephacryl S-200, hypatite C
-
native enzyme from strain BL21(DE3), 730fold to homogeneity by ammonium sulfate fractionation, DEAE ion exchange and Red-A affinity chromatography, ultrafiltration, hypatite C-resin chromatography, and a second ultrafiltration step
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant isoenzyme A, Red A dye-affinity, anion exchange, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CTATCC11996_22452, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene dkr, recombinant expression in Lactococcus lactis subsp. cremoris strains MG1363 or NZ3900 and Lactobacillus plantarum strain WCFS1 using food-grade vectors
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is significantly induced by estrone, estradiol, and methyltestosterone, and slightly by progesterone, but not by testosterone
the enzyme expression is significantly induced by estrone, estradiol, and methyltestosterone, and slightly by progesterone, but not by testosterone
-
the enzyme expression is significantly induced by estrone, estradiol, and methyltestosterone, and slightly by progesterone, but not by testosterone
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
enzyme is a target for the construction of a NADH-utilizing mutant strain in the industrial production of vitamin C
synthesis
synthesis
enzyme may be useful for the synthesis of the ascorbate precursor 2-keto-L-gulonate
synthesis
enzyme can be used in the industrial production of vitamin C
synthesis
enzymatic production of the vitamin C precursor 2-keto-L-gulonate (2-KLG) from 2,5-diketo-D-gluconate (2,5-DKG) by coupling 2,5-diketo-D-gluconic acid reductase via its coenzyme to glucose dehydrogenase. The bienzymatic process shows complicated inhibition patterns caused by reaction products, NADP+ and NADPH. The key parameters for a fast and efficient conversion are the NADP(H) concentration, the volumetric activity of 2,5-DKG reductase, the ratio of synthetic enzyme activity to regenerate enzyme activity and the glucono-1,5-lactone concentration. By modeling the space-time yield of the process is nearly doubled and the coenzyme concentration reduced threefold
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.1.274)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
