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Information on EC 1.1.1.274 - 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)
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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).
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Word Map
- 1.1.1.274
-
2,5-diketo-d-gluconic
-
2-keto-l-gulonic
- corynebacterium
-
nadph-dependent
-
aldo-keto
-
l-ascorbic
- d-glucose
- citrinum
-
cofactor-binding
-
activity-stained
- aldose
-
penicillium
- synthesis
- ascorbate
- erwinia
-
error-prone
-
stereo-specific
- citrea
-
two-phase
-
pantoea
-
enantioselectivity
-
biocatalysis
- 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
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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
YqhE reductase
-
-
-
-
2,5-diketo-D-gluconate reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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+
reaction 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+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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).
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CAS REGISTRY NUMBER
COMMENTARY
95725-95-4
-
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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+
-
-
-
-
-
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+
H1RW56
-
-
-
?
2-dehydro-D-gulonate + NADP+
2,5-didehydro-D-gluconate + NADPH + H+
H1RW56
-
-
-
?
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
?
-
H1RW56
the enzyme catalyzes degradation of estradiol, estrone, testosterone, and methyltestosterone, overview
-
-
-
additional information
?
-
H1RW56
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
-
-
-
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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+
P06632
step in the biosynthesis of L-ascorbic acid
-
-
?
2,5-didehydro-D-gluconate + NADPH + H+
2-dehydro-D-gluconate + NADP+
H9CWC0
-
-
-
?
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+
H1RW56
-
-
-
?
2-dehydro-D-gulonate + NADP+
2,5-didehydro-D-gluconate + NADPH + H+
H1RW56
-
-
-
?
additional information
?
-
H1RW56
the enzyme catalyzes degradation of estradiol, estrone, testosterone, and methyltestosterone, overview
-
-
-
additional information
?
-
H1RW56
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
-
-
-
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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
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,5-didehydro-D-gluconate
substrate inhibition of isozyme B, not of isozyme A, at high concentrations
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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; K232G/R238H 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; F22Y/K232G/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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18.3
NADPH
-
F22Y/A272G isoenzyme A mutant; F22Y/K232G/R235G/R238H/A272G isoenzyme A mutant
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
-
YafB, 10 mM D-xylose as substrate; YafB, 1 mM 2-carboxybenzaldehyde as substrate; YqhE, 1 mM 2-carboxybenzaldehyde as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
H1RW56
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
H1RW56
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
H1RW56
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 (2257 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
34000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
H1RW56
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
-
monomer
-
1 * 29992, deduced from nucleotide sequence; 1 * 34000, SDS-PAGE
monomer
-
1 * 29992, deduced from nucleotide sequence; 1 * 34000, SDS-PAGE
-
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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
-
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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
-
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
H1RW56
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
-
mutagenesis of 3 amino acids in the cofactor-binding pocket, mutations lead to higher activity with NADH as cofactor
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
thermodynamic stability study of wild-type and F22Y/K232G/R238H/A272G mutant enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme, 400 mM potassium phoshate buffer, pH 7.0, several weeks without appreciable loss of activity
-
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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
H1RW56
recombinant isoenzyme A, Red A dye-affinity, anion exchange, gel filtration
-
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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)
H1RW56
gene dkr, recombinant expression in Lactococcus lactis subsp. cremoris strains MG1363 or NZ3900 and Lactobacillus plantarum strain WCFS1 using food-grade vectors
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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
H1RW56
the enzyme expression is significantly induced by estrone, estradiol, and methyltestosterone, and slightly by progesterone, but not by testosterone
-
-
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sonoyama, T.; Kobayashi, K.
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