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Information on EC 1.1.1.15 - D-iditol 2-dehydrogenase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.1.1.15
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RECOMMENDED NAME
GeneOntology No.
D-iditol 2-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-iditol + NAD+ = D-sorbose + NADH + H+
Also converts xylitol into L-xylulose and L-glucitol into L-fructose
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
D-iditol:NAD+ 2-oxidoreductase
Also converts xylitol into L-xylulose and L-glucitol into L-fructose.
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CAS REGISTRY NUMBER
COMMENTARY
9028-22-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
evolution
the enzyme BjSDH is part of the superfamily of Zn-independent short-chain dehydrogenases. The BjSDH structure folds in the Rossmann fold, which is typical for NADH-dependent enzymes and the SDR family
evolution
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the enzyme BjSDH is part of the superfamily of Zn-independent short-chain dehydrogenases. The BjSDH structure folds in the Rossmann fold, which is typical for NADH-dependent enzymes and the SDR family
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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
D-iditol + NAD+
D-sorbose + NADH
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less stable enzyme, dulcitol-inducible, accounts for oxidation of certain fully hydroxylated polyols containing a D-threo-configuration adjacent to a primary alcohol
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?
D-iditol + NAD+
D-sorbose + NADH + H+
i.e. D-sorbitol
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r
D-iditol + NAD+
D-sorbose + NADH + H+
i.e D-sorbitol
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r
L-glucitol + NAD+
D-sorbose + NADH + H+
i.e. D-sorbitol, 90% conversion of L-glucitol to D-sorbose
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r
L-glucitol + NAD+
D-sorbose + NADH + H+
i.e. D-sorbitol, 90% conversion of L-glucitol to D-sorbose
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r
additional information
?
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the substrate in BjSDH is stabilized via the side chain of Glu150, Ser140 and the carbonyl groups of Pro183 and Gly184
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additional information
?
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the substrate in BjSDH is stabilized via the side chain of Glu150, Ser140 and the carbonyl groups of Pro183 and Gly184
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
D-iditol + NAD+
D-sorbose + NADH
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less stable enzyme, dulcitol-inducible, accounts for oxidation of certain fully hydroxylated polyols containing a D-threo-configuration adjacent to a primary alcohol
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?
D-iditol + NAD+
D-sorbose + NADH + H+
Q89FN7
i.e. D-sorbitol
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
additional information
a continuous beta-sheet is formed between two monomers in the tetramer. The BjSDH structure folds in the Rossmann fold. The monomer of BjSDH is composed of a central parallel beta-sheet surrounded by three alpha-helices on each side. At the top of the beta-sheet a small helix–turn–helix motif is located between the two final beta-strands betaF and betaG. Tetrameric quaternary organization, structure comparisons, overview
additional information
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a continuous beta-sheet is formed between two monomers in the tetramer. The BjSDH structure folds in the Rossmann fold. The monomer of BjSDH is composed of a central parallel beta-sheet surrounded by three alpha-helices on each side. At the top of the beta-sheet a small helix–turn–helix motif is located between the two final beta-strands betaF and betaG. Tetrameric quaternary organization, structure comparisons, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme in complex with both NAD+ and glucitol, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement and modelling
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21-Gold (DE3) by heat treatment at 50°C and metal affinity chromatography to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene rdh, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-Gold (DE3)
gene SDh, DNA and amino acid sequence determination and analysis, isolation, characterization and evaluation of the Pichia pastoris sorbitol dehydrogenase promoter for expression of heterologous proteins, recombinant expression of several different enzymes using the SDH promoter, overview
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.15)
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