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Information on EC 1.1.1.15 - D-iditol 2-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.15
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.15 D-iditol 2-dehydrogenase
IUBMB Comments
Also converts xylitol into L-xylulose and L-glucitol into L-fructose.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
BjSDH, D-sorbitol dehydrogenase, SDH, sorbitol dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BjSDH
D-sorbitol dehydrogenase
SDH
sorbitol dehydrogenase
D-sorbitol dehydrogenase
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-
-
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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
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-iditol + NAD+
D-sorbose + NADH
-
Substrates: less stable enzyme, dulcitol-inducible, accounts for oxidation of certain fully hydroxylated polyols containing a D-threo-configuration adjacent to a primary alcohol
Products: -
Products: -
?
D-glucitol + NAD+
D-fructose + NADH + H+
Substrates: -
Products: -
Products: -
r
D-glucitol + NAD+
D-fructose + NADH + H+
Substrates: -
Products: -
Products: -
r
D-iditol + NAD+
D-sorbose + NADH + H+
Substrates: i.e. D-sorbitol
Products: -
Products: -
r
D-iditol + NAD+
D-sorbose + NADH + H+
Substrates: i.e D-sorbitol
Products: -
Products: -
r
D-iditol + NAD+
D-sorbose + NADH + H+
Substrates: i.e. D-sorbitol
Products: -
Products: -
r
D-iditol + NAD+
D-sorbose + NADH + H+
Substrates: i.e D-sorbitol
Products: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-glucitol + NAD+
D-sorbose + NADH + H+
Substrates: i.e. D-sorbitol, 90% conversion of L-glucitol to D-sorbose
Products: -
Products: -
r
L-glucitol + NAD+
D-sorbose + NADH + H+
Substrates: i.e. D-sorbitol, 90% conversion of L-glucitol to D-sorbose
Products: -
Products: -
r
additional information
?
-
Substrates: the substrate in BjSDH is stabilized via the side chain of Glu150, Ser140 and the carbonyl groups of Pro183 and Gly184
Products: -
Products: -
?
additional information
?
-
Substrates: the substrate in BjSDH is stabilized via the side chain of Glu150, Ser140 and the carbonyl groups of Pro183 and Gly184
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-iditol + NAD+
D-sorbose + NADH
-
Substrates: less stable enzyme, dulcitol-inducible, accounts for oxidation of certain fully hydroxylated polyols containing a D-threo-configuration adjacent to a primary alcohol
Products: -
Products: -
?
D-iditol + NAD+
D-sorbose + NADH + H+
Substrates: i.e. D-sorbitol
Products: -
Products: -
r
D-iditol + NAD+
D-sorbose + NADH + H+
Substrates: i.e. D-sorbitol
Products: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q89FN7_BRADU
Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
242
0
26089
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
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 helixturnhelix motif is located between the two final beta-strands betaF and betaG. Tetrameric quaternary organization, structure comparisons, overview
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 helixturnhelix 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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shaw, D.R.D.
Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol dehydrogenase
Biochem. J.
64
394-405
1956
Pseudomonas sp.
brenda
Fredslund, F.; Otten, H.; Gemperlein, S.; Poulsen, J.C.; Carius, Y.; Kohring, G.W.; Lo Leggio, L.
Structural characterization of the thermostable Bradyrhizobium japonicum D-sorbitol dehydrogenase
Acta Crystallogr. Sect. F
72
846-852
2016
Bradyrhizobium japonicum (Q89FN7), Bradyrhizobium japonicum USDA110 (Q89FN7)
brenda
Periyasamy, S.; Govindappa, N.; Sreenivas, S.; Sastry, K.
Isolation, characterization and evaluation of the Pichia pastoris sorbitol dehydrogenase promoter for expression of heterologous proteins
Protein Expr. Purif.
92
128-133
2013
Komagataella pastoris, Komagataella pastoris BICC 9450
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.15)
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