Information on EC 1.1.1.384 - dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.384
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RECOMMENDED NAME
GeneOntology No.
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+ = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dTDP-beta-L-digitoxose biosynthesis
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dTDP-D-forosamine biosynthesis
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dTDP-D-olivose, dTDP-D-oliose and dTDP-D-mycarose biosynthesis
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dTDP-L-olivose biosynthesis
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dTDPLrhamnose biosynthesis
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Polyketide sugar unit biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose:NADP+ 3-oxidoreductase
The enzyme is involved in the biosynthesis of several deoxysugars, including L-digitoxose, L- and D-olivose, L-oliose, D-mycarose and forosamine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Q9ALN5
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
show the reaction diagram
dTDP-3-dehydro-6-deoxy-alpha D-galactose + NADPH + H+
dTDP-fucose + NADP+
show the reaction diagram
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?
dTDP-3-dehydro-6-deoxy-alpha-D-glucose + NADPH + H+
dTDP-quinovose + NADP+
show the reaction diagram
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?
TDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
TDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
show the reaction diagram
additional information
?
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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
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
show the reaction diagram
B3TMR8
the enzyme is involved in the biosynthesis of dTDP-L-digitoxose
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?
TDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
TDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
show the reaction diagram
Q9ALN5
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
Q9ALN5
NADPH is preferred over NADH
NADPH
Q9ALN5
preferred over NADH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35834
x * 35834, calculated
37732
Q9ALN5
1 * 38000, SDS-PAGE, 1 * 37732, calculated, His-tagged recombinant protein
38000
Q9ALN5
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35834, calculated
monomer
Q9ALN5
1 * 38000, SDS-PAGE, 1 * 37732, calculated, His-tagged recombinant protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop method of vapor diffusion, binary and ternary complexes of KijD10 with NADP+ and dTDP-benzene, 2.0 A resolution or better
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Streptomyces albus
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the genes required for the biosynthesis of dTDP-L-olivose and dTDP-L-oleandrose in Streptomyces albus and incubation with the erythromycin aglycon erythronolide B gives rise to L-3-O-olivosyl- and L-3-O-oleandrosyl-erythronolide B
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K102A
mutant protein is completely inactive
K102E
mutant enzyme retains some activity, but its catalytic efficiency is reduced by more than 4 orders of magnitude from that for the wild-type enzyme
K102M
mutant protein is completely inactive
K102Q
mutant protein is completely inactive