Information on EC 1.17.1.1 - CDP-4-dehydro-6-deoxyglucose reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.17.1.1
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RECOMMENDED NAME
GeneOntology No.
CDP-4-dehydro-6-deoxyglucose reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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CDP-4-dehydro-3,6-dideoxy-D-glucose biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-87-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O
show the reaction diagram
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biosynthesis of 3,6-dideoxysugars
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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the second substrate of the reaction, the hydrogen donor
NADPH
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
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
iodoacetamide
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85% inhibition at 100 mM
N-ethylmaleimide
p-chloromercuribenzoate
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91% inhibition at 1 mM
p-Chlorophenylsulfonate
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91% inhibition at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
CDP-4-keto-6-deoxy-D-glucose
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
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pH 5.5: about 60% of activity maximum, pH 8.5: about 40% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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; 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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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information