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EC Tree
IUBMB Comments The enzyme consists of two proteins. One forms an enzyme-bound adduct of the CDP-4-dehydro-6-deoxyglucose with pyridoxamine phosphate, in which the 3-hydroxy group has been removed. The second catalyses the reduction of this adduct by NAD(P)H and release of the CDP-4-dehydro-3,6-dideoxy-D-glucose and pyridoxamine phosphate.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
ascD, CDP-4-keto-6-deoxy-D-glucose-3-dehydrogenase system, CDP-4-keto-deoxy-glucose reductase, CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase, cytidine diphosphate 4-keto-6-deoxy-D-glucose-3-dehydrogenase, More, NAD(P)H:CDP-4-keto-6-deoxy-D-glucose oxidoreductase, reductase, cytidine diphospho-4-keto-6-deoxy-D-glucose, rfbH,
more
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CDP-4-keto-6-deoxy-D-glucose-3-dehydrogenase system
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CDP-4-keto-deoxy-glucose reductase
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CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
cytidine diphosphate 4-keto-6-deoxy-D-glucose-3-dehydrogenase
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NAD(P)H:CDP-4-keto-6-deoxy-D-glucose oxidoreductase
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reductase, cytidine diphospho-4-keto-6-deoxy-D-glucose
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ascD
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CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
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CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
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CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
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CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
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rfbH
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additional information
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2 proteins E1 and E3 are involved but no partial reaction has been observed in the presence of either alone
additional information
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2 proteins E1 and E3 are involved but no partial reaction has been observed in the presence of either alone
additional information
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2 proteins E1 and E3 are involved but no partial reaction has been observed in the presence of either alone
additional information
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2 proteins E1 and E3 are involved but no partial reaction has been observed in the presence of either alone
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
mechanism
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
mechanism
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
E1 binds the substrate pyridoxamine 5'-phosphate essential for binding, E3 possesses NADH oxidase activity, may be the reductase
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
2 proteins, E1 and E3, are involved but no partial reaction is observed in the presence of either alone
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
2 proteins, E1 and E3, are involved but no partial reaction is observed in the presence of either alone
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
role of the enzymes E1 and E3, as well as role of the cofactor. Multicomponent system consisting of substrate, NADH or NADPH, enzyme E1: recognition unit of the system by binding to the substrate through the amino group of the coenzyme, enzyme E3: acts as the dehydrogenase of the system, and cofactor: pyridoxamine 5'-phosphate
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
mechanism
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
2 proteins, E1 and E3, are involved but no partial reaction is observed in the presence of either alone
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
E1 binds the substrate pyridoxamine 5'-phosphate essential for binding, E3 possesses NADH oxidase activity, may be the reductase
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
role of the enzymes E1 and E3, as well as role of the cofactor. Multicomponent system consisting of substrate, NADH or NADPH, enzyme E1: recognition unit of the system by binding to the substrate through the amino group of the coenzyme, enzyme E3: acts as the dehydrogenase of the system, and cofactor: pyridoxamine 5'-phosphate
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
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CDP-4-dehydro-3,6-dideoxy-D-glucose:NAD(P)+ 3-oxidoreductase
The enzyme consists of two proteins. One forms an enzyme-bound adduct of the CDP-4-dehydro-6-deoxyglucose with pyridoxamine phosphate, in which the 3-hydroxy group has been removed. The second catalyses the reduction of this adduct by NAD(P)H and release of the CDP-4-dehydro-3,6-dideoxy-D-glucose and pyridoxamine phosphate.
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
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r
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
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?, r
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
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?, r
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
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?, r
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
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?, r
CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O
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CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O
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CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O
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the substrate undergoes substitution of a hydroxyl group by a hydrogen atom at carbon atom 3 from glucose, it is supposed that the reaction is triggered by an attack from a hydride ion from NAD(P)H to atom carbon 3
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CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O
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biosynthesis of 3,6-dideoxysugars
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CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O
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biosynthesis of 3,6-dideoxysugars
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
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CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD+ + H2O
CDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
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pyridoxamine 5'-phosphate
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bound to enzyme E1 through an ionic interaction with a positive charge on the surface of the enzyme, the cofactor is needed for the binding of the substrate to the enzyme
NAD+
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NADH
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NADH
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the second substrate of the reaction, the hydrogen donor
NADPH
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NADPH
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the second substrate of the reaction, the hydrogen donor
additional information
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4.3 SH per mol of enzyme E1 in the presence of SDS, calculated using a molecular weight of 61000 Da
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additional information
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3.8 SH groups per molecule of enzyme E1, in the presence and absence of SDS
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additional information
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0.37 SH groups per molecule of enzyme E3, in the absence of SDS and 1 SH group per molecule of enzyme E3 in the presence of SDS, the single SH group in enzyme E3 is essential for activity
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additional information
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0.37 SH groups per molecule of enzyme E3, in the absence of SDS and 1 SH group per molecule of enzyme E3 in the presence of SDS, the single SH group in enzyme E3 is essential for activity
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additional information
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derivatives of vitamin B6 such as pyridoxine, pyridoxine 5'-phosphate, pyridoxal, pyridoxal 5'-phosphate, pyridoxamine and pyridoxamine 5'-phosphate have stimulatory effect on the reaction, indicating that the amino group and the phosphate group are necessary for the reaction
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additional information
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no divalent cation required
additional information
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no divalent cation required
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5,5'-dithiobis(2-nitrobenzoate)
iodoacetamide
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85% inhibition at 100 mM
p-chloromercuribenzoate
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91% inhibition at 1 mM
p-Chlorophenylsulfonate
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91% inhibition at 1 mM
ZINC03201893
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inhibits CDP-4-dehydro-6-deoxyglucose reductase
ZINC03831425
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inhibits CDP-4-dehydro-6-deoxyglucose reductase
ZINC03831426
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inhibits CDP-4-dehydro-6-deoxyglucose reductase
ZINC03831427
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inhibits CDP-4-dehydro-6-deoxyglucose reductase
ZINC03831428
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inhibits CDP-4-dehydro-6-deoxyglucose reductase
ZINC08551105
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inhibits CDP-4-dehydro-6-deoxyglucose reductase
ZINC08551106
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inhibits CDP-4-dehydro-6-deoxyglucose reductase
ZINC08551107
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inhibits CDP-4-dehydro-6-deoxyglucose reductase
5,5'-dithiobis(2-nitrobenzoate)
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inhibits the activity of the whole system
5,5'-dithiobis(2-nitrobenzoate)
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89% inhibition at 10 mM
5,5'-dithiobis(2-nitrobenzoate)
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N-ethylmaleimide
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inhibits the activity of the whole system
N-ethylmaleimide
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88% inhibition at 10 mM
N-ethylmaleimide
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enzyme E1: dithiothreitol in excess protects against inhibition
ZINC00020252
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC00020252
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC00057147
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC00057147
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC00057347
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC00057347
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC00057358
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC00057358
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC03794794
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC03794794
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC03830609
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC03830609
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC06507052
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC06507052
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC12503116
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC12503116
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC20444132
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
ZINC20444132
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inhibits CDP-6-deoxy-D-xylo-4-hexulose-3-dehydrase
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0.15
CDP-4-keto-6-deoxy-D-glucose
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additional information
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additional information
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additional information
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5.5 - 8.5
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pH 5.5: about 60% of activity maximum, pH 8.5: about 40% of activity maximum
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brenda
gene rfbH
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brenda
gene rfbH
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brenda
gene ascD
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brenda
25 VO
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brenda
gene ascD
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brenda
LT-2
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brenda
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brenda
25 VO
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brenda
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35000 - 45000
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enzyme E3, thin-layer chromatography on Sephadex G-100
40000
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enzyme E3: 1 * 40000, SDS-PAGE, enzyme E1: 1 * 61000, SDS-PAGE, 2 proteins E1 and E3 are involved but no partial reaction has been observed in the presence of either alone
50000 - 70000
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enzyme E1, thin-layer chromatography on Sephadex G-100
60000 - 70000
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enzyme E1, thin-layer chromatography on Sephadex G-100
61000
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enzyme E3: 1 * 40000, SDS-PAGE, enzyme E1: 1 * 61000, SDS-PAGE, 2 proteins E1 and E3 are involved but no partial reaction has been observed in the presence of either alone
additional information
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cofactor: 200-400, gel filtration on Bio Gel P2
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monomer
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enzyme E3: 1 * 40000, SDS-PAGE, enzyme E1: 1 * 61000, SDS-PAGE, 2 proteins E1 and E3 are involved but no partial reaction has been observed in the presence of either alone
monomer
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enzyme E3: 1 * 40000, SDS-PAGE, enzyme E1: 1 * 61000, SDS-PAGE, 2 proteins E1 and E3 are involved but no partial reaction has been observed in the presence of either alone
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additional information
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enzyme structure prediction, model
additional information
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enzyme structure prediction, model
additional information
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enzyme structure prediction, model
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additional information
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enzyme structure prediction, model
additional information
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enzyme structure prediction, model
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additional information
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a mutant which cannot synthesize CDP-abequose is found to be missing E1
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frozen, for months without loss of activity, enzyme E1
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lyophilized powder: enzyme E3 not stable
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lyophilized powder: for months, enzyme E1
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enzyme E1: using filtration on a Sephadex G-100 column and column chromatography on DEAE-cellulose, enzyme E3: using two filtrations on Sephadex G-100 columns
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of cofactor, using streptomycin sulfate precipitation, ammonium sulfate precipitation and dialysis, DEAE-cellulose chromatography, ultrafiltration, Bio Gel P-2 filtration and ion exchange chromatography on Dowex-1
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the first three steps are common to the purification of enzyme E1, enzyme E3 and cofactor, their separation can be accomplished after step 4, step 1: preparation of the crude extract, step 2: streptomycin sulfate precipitation, step 3: ammonium sulfate precipitation and dialysis, step 4: DEAE-cellulose chromatography, step 5: purification of enzyme E1, gel filtration on Sephadex G-100, step 6: second DEAE-cellulose chromatography, step 7: preparative polyacrylamide gel electrophoresis, step 5': purification of enzyme E3, gel filtration on Sephadex G-100, step 6': second DEAE-cellulose chromatography, step 7': third DEAE-cellulose chromatography
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gene ascD, sequence analysis and comparisons
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gene rfbH, sequence analysis and comparisons
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sequence analysis and comparisons
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drug development
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the enzyme is a drug target
drug development
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the enzyme is a drug target
drug development
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the enzyme is a drug target
drug development
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the enzyme is a drug target
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drug development
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the enzyme is a drug target
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Gonzalez-Porque, P.
Cytidine diphosphate 4-keto-6-deoxy-D-glucose-3-dehydrogenase
Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York
1
391-419
1986
Yersinia pseudotuberculosis
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brenda
Pape, H.; Strominger, J.L.
Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. V. Partial purification of the two protein components required for introduction of the 3-deoxy group
J. Biol. Chem.
244
3598-3604
1969
Yersinia pseudotuberculosis, Salmonella enterica subsp. enterica serovar Typhimurium, Yersinia pseudotuberculosis 25VO
brenda
Gonzalez-Porque, P.; Strominger, J.L.
Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. VI. Purification to homogeneity and some properties of cytidine diphosphate-D-glucose oxidoreductase, enzyme E1 and enzyme E3
J. Biol. Chem.
247
6748-6756
1972
Yersinia pseudotuberculosis, Yersinia pseudotuberculosis 25VO
brenda
Verma, A.; Goel, N.; Laxmi, V.; Rathi, B.; Sharda, S.
Elucidating vital drug targets of Salmonella enterica utilizing the bioinformatic approach
J. Pharm. Sci. Res.
8
71-78
2016
Salmonella enterica, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Gallinarum, Salmonella enterica subsp. enterica serovar Gallinarum SG9, Salmonella enterica subsp. enterica serovar Typhimurium DT104
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brenda
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