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Information on EC 1.1.1.14 - L-iditol 2-dehydrogenase
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1.1.1.14 L-iditol 2-dehydrogenaseIUBMB Comments
This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. Enzymes from different organisms or tissues display different substrate specificity. The enzyme is specific to NAD+ and can not use NADP+.
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Word Map
- 1.1.1.14
- polyols
- aminotransferase
-
hepatotoxicity
- aldose
- fructose
- necrosis
- transaminase
- dehydrogenases
- sheep
- lens
-
alt
- bile
- bilirubin
- testicular
- cataract
-
gamma-glutamyl
- ccl4
-
tetrachloride
- acetaminophen
- transpeptidase
- gluconobacter
- xylitol
- oxydans
-
centrilobular
-
hepatoprotective
- galactitol
- bromobenzene
- ribitol
- apap
-
forestomach
- l-sorbose
-
acetaminophen-induced
-
pneumotoxicity
-
hepatotoxicants
-
glutamic-pyruvic
- d-mannitol
- aminopyrine
-
diapause
- sorbinil
- n-demethylase
-
13-week
- fructokinase
- synthesis
- medicine
- agriculture
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ADH, D-sorbitol dehydrogenase, dehydrogenase, L-iditol, Dgeo_2865, glucitol dehydrogenase, GoSCR, L-iditol 2-dehydrogenase, L-iditol dehydrogenase (sorbitol), L-iditol:NAD oxidoreductase, L-iditol:NAD+ 5-oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-sorbitol dehydrogenase
dehydrogenase, L-iditol
-
-
-
-
Dgeo_2865
glucitol dehydrogenase
-
-
-
-
GoSCR
L-iditol 2-dehydrogenase
-
-
-
-
L-iditol dehydrogenase (sorbitol)
-
-
-
-
L-iditol:NAD oxidoreductase
-
-
-
-
L-iditol:NAD+ 5-oxidoreductase
-
-
-
-
NAD+-dependent sorbitol dehydrogenase
NAD-dependent sorbitol dehydrogenase
-
-
-
-
NAD-sorbitol dehydrogenase
-
-
-
-
PDH-11300
polyol dehydrogenase
Protein tms1
-
-
-
-
SDH
SldA
SLDH
sorbitol dehydrogenase
SORD
additional information
NAD+-dependent sorbitol dehydrogenase
-
-
-
-
polyol dehydrogenase
-
-
-
-
sorbitol dehydrogenase
-
-
-
-
additional information
-
enzyme belongs to the family of medium-chain dehydrogenase/reductase proteins
additional information
-
enzyme belongs to the family of medium-chain dehydrogenase/reductase proteins
additional information
-
enzyme belongs to the family of medium-chain dehydrogenase/reductase proteins
additional information
-
enzyme belongs to the family of medium-chain dehydrogenase/reductase proteins
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-iditol + NAD+ = L-sorbose + NADH + H+
-
-
-
-
L-iditol + NAD+ = L-sorbose + NADH + H+
ordered catalytic mechanism and substrate binding
-
L-iditol + NAD+ = L-sorbose + NADH + H+
ordered catalytic mechanism and substrate binding
-
L-iditol + NAD+ = L-sorbose + NADH + H+
ordered catalytic mechanism and substrate binding
-
L-iditol + NAD+ = L-sorbose + NADH + H+
ordered catalytic mechanism and substrate binding, active site structure
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
L-iditol:NAD+ 2-oxidoreductase
This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. Enzymes from different organisms or tissues display different substrate specificity. The enzyme is specific to NAD+ and can not use NADP+.
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CAS REGISTRY NUMBER
COMMENTARY
9028-21-1
-
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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
6-deoxy-D-sorbitol + NAD+
? + NADH
-
nearly 2fold higher activity compared to D-sorbitol
-
-
?
6-fluoro-D-sorbitol + NAD+
? + NADH
-
over 2fold higher activity compared to D-sorbitol, best substrate
-
-
?
D-sorbitol + 2,6-dichlorophenolindophenol
L-sorbose + ?
-
electron acceptor: i.e. DCIP
-
-
?
D-xylitol + NADP+
? + NADPH + H+
NADP+ is not a cofactor for wild-type, but for a substrate-binding loop chimera
-
-
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
-
-
-
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
99% enantiomeric excess
-
-
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
-
-
-
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
99% enantiomeric excess
-
-
?
D-arabitol + NAD(P)+
D-xylulose + NAD(P)H + H+
-
-
-
?
D-arabitol + NAD+
?
Luteovulum sphaeroides Si4 / DSM 8371
-
D-arabinitol is identical, low activity
-
-
?
D-arabitol + NAD+
D-xylulose + NADH + H+
-
best substrate
-
-
?
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
-
-
-
?
D-sorbitol + NAD(P)+
L-sorbose + NAD(P)H + H+
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
second step of the polyol pathway of glucose metabolism, important in diabetic disease and hyperglycaemia
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
i.e. D-glucitol, dissociation of the enzyme-coenzyme binary complex is the rate-limiting step, interaction of Zn2+ with Ser46 and the oxygen atom of the 2-hydroxy and the 4-hydroxy groups is important for substrate binding
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
Luteovulum sphaeroides Si4 / DSM 8371
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
second step of the polyol pathway of glucose metabolism
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
i.e. D-glucitol, dissociation of the enzyme-coenzyme binary complex is the rate-limiting step
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
second step of the polyol pathway of glucose metabolism
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
i.e. D-glucitol, dissociation of the enzyme-coenzyme binary complex is the rate-limiting step, 2- and 4-hydroxy groups of D-sorbitol are important for substrate bindig
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
second step of the polyol pathway of glucose metabolism
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
i.e. D-glucitol, dissociation of the enzyme-coenzyme binary complex is the rate-limiting step
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
enzyme is the main L-sorbose producing activity in the cell
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
enzyme is the main L-sorbose producing activity in the cell
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
part of the polyol pathway that interconverts glucose and fructose
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
the primary enzyme responsible for metabolism of the major phloem-transported carbohydrate sorbitol, present and active during apple fruit set and early development
-
-
?
additional information
?
-
-
no activity with D-glucose, D-fructose, L-sorbose, methanol, ethanol, and sucrose
-
-
?
additional information
?
-
no activity against D-xylitol, D-ribitol, D-inositol or glycerol
-
-
?
additional information
?
-
-
no activity against D-xylitol, D-ribitol, D-inositol or glycerol
-
-
?
additional information
?
-
an enantiocomplementary carbonyl reductase, polyol dehydrogenase (GoSCR) from Gluconobacter oxydans is discovered to convert 2-hydroxyacetophenone (2-HAP) to (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity. No activity with NADPH
-
-
-
additional information
?
-
an enantiocomplementary carbonyl reductase, polyol dehydrogenase (GoSCR) from Gluconobacter oxydans is discovered to convert 2-hydroxyacetophenone (2-HAP) to (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity. No activity with NADPH
-
-
-
additional information
?
-
no activity against D-xylitol, D-ribitol, D-inositol or glycerol
-
-
?
additional information
?
-
-
no activity against D-xylitol, D-ribitol, D-inositol or glycerol
-
-
?
additional information
?
-
-
no activity with D-glucose, D-fructose, L-sorbose, methanol, ethanol, and sucrose
-
-
?
additional information
?
-
-
no activity with 2-deoxy-D-sorbitol and 2-fluoro-D-sorbitol, 3-fluoro-D-sorbitol and 4-fluoro-D-sorbitol are poor substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
-
-
-
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
second step of the polyol pathway of glucose metabolism, important in diabetic disease and hyperglycaemia
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
second step of the polyol pathway of glucose metabolism
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
second step of the polyol pathway of glucose metabolism
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
second step of the polyol pathway of glucose metabolism
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
enzyme is the main L-sorbose producing activity in the cell
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
enzyme is the main L-sorbose producing activity in the cell
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
part of the polyol pathway that interconverts glucose and fructose
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
the primary enzyme responsible for metabolism of the major phloem-transported carbohydrate sorbitol, present and active during apple fruit set and early development
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
285872, 285873, 285878, 285880, 285882, 285883, 285889, 285891, 285893, 285894, 285900, 655289, 684974
NADH
-
-
NADP+
exhibits 15 times higher activity in the presence of NADP+ than that of NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn
Zn2+
Zn2+
-
1 catalytic zinc atom per subunit, interaction with Ser46 and the oxygen atom of the 2-hydroxy and the 4-hydroxy groups is important for substrate binding
Zn2+
the catalytic zinc is coordinated with residues His69, Cys44, Glu70, and a water molecule
Zn2+
-
apparent stability constant of 1600000000000 per M for Zn(II)Ć¢ĀĀSDH. Under physiological conditions, enzyme is saturated with Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-methyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
i.e. SDI-157
CP-642,931
-
a potent and specific sorbitol dehydrogenase inhibitor, rmacokinetics, biomarker pharmacodynamics, and safety analysis, overview. The inhibitor is rapidly absorbed through the oral route and effectively inhibits SDH. However, the drug is not well tolerated due to adverse neuromuscular effects. The inhibitor alters the red blood cell sorbitol dehydrogenase activity after oral administration
dithioerythritol
-
protection at low concentration, inhibition at high concentration, 100 mM
DTT
-
competitive and noncompetitive with respect to D-sorbitol and NAD+, respectively
2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
-
i.e. SDI-158
2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
i.e. SDI-158 or CP-166,572
2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
-
i.e. SDI-158, inhibition mechanism, dissociation constants of enzyme-inhibitor complex at various pH values
2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
-
i.e. SDI-158
cysteine
-
strong effect on sorbitol oxidation, slight effect on fructose reduction, ZnSO4 reverses inhibition
dithiothreitol
-
protection at low concentration, inhibition at high concentration, 100 mM
iodoacetate
-
strong effect on sorbitol oxidation, weaker effect on fructose reduction
additional information
-
inhibition mechanism, poor inhibitors are 3,4-dihydroxyphenyl-ethandiol, imidazole, isobutyramide, and urea
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme needs product, i.e. SldB, of upstream gene sldB, encoding a hydrophobic polypeptide, for activity, the polypeptide might be a chaperone-like component that signals processing and folding of the enzyme to give the active enzyme form
-
additional information
-
enzyme needs product, i.e. SldB, of upstream gene sldB, encoding a hydrophobic polypeptide, for activity, the polypeptide might be a chaperone-like component that signals processing and folding of the enzyme to give the active enzyme form
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
2-hydroxyacetophenone
pH 7.0, 25ĆĀ°C, recombinant His-tagged enzyme
0.41
NADP+
substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication
18
D-sorbitol
-
pH 6.0, 25ĆĀ°C, with 2,6-dichlorophenolindophenol as electron acceptor
0.15
NAD+
wild-type, pH 9.0, temperature not specified in the publication
0.15
NAD+
substrate-binding loop chimera, pH 9.0, temperature not specified in the publication
0.44
NAD+
substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.42
NADP+
substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication
1.53
NAD+
substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication
1.61
NAD+
wild-type, pH 9.0, temperature not specified in the publication
2.7
NAD+
substrate-binding loop chimera, pH 9.0, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.45
NADP+
substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication
3.48
NAD+
substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication
10.74
NAD+
wild-type, pH 9.0, temperature not specified in the publication
17.8
NAD+
substrate-binding loop chimera, pH 9.0, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics at different pH
-
0.00023
2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
-
-
0.00025
2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1013
substrate 1,2-butanediol, wild-type, pH 9.0, temperature not specified in the publication
1427
substrate D-galactitol, wild-type, pH 9.0, temperature not specified in the publication
2742
substrate 1,2-hexanediol, wild-type, pH 9.0, temperature not specified in the publication
4659
substrate D-xylitol, wild-type, pH 9.0, temperature not specified in the publication
936
substrate D-sorbitol, wild-type, pH 9.0, temperature not specified in the publication
additional information
-
activity at growth in media with different pH values
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11
7.4
9 - 10
9.5
9.6
9.9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7 - 8
-
at pH 4.7 and 8 about 50% of activity maximum, D-fructose reduction
5 - 7
5 - 7.5
-
less than 20% of maximal activity below pH 5, less than 80% above pH 7.5, fructose reduction
6 - 7.2
-
less than 50% of maximal activity above and below, sugar reduction
6 - 9
-
at pH 6 about 70% of maximal activity, at pH 9 about 40%, fructose reduction
7 - 10
-
40% of maximal activity at 7 and 70% of maximal activity at 10, sorbitol oxidation
7.5 - 10
-
at pH 7.5 about 70% of maximal activity, at pH 10 about 100%, sorbitol oxidation
7.5 - 9
-
less than 20% of maximal activity below pH 7.5, 100% at pH 9.0, sorbitol oxidation
7.5 - 9.5
-
at pH 7.5 and pH 9.5 about 70% of maximal activity, sorbitol oxidation
9 - 10.5
-
less than 70% of maximal activity above and below, sorbitol oxidation
9.2 - 11.6
-
less than 50% of maximal activity above and below, sorbitol oxidation
additional information
5 - 7
-
30% of maximal activity at pH 5.0 and 60% of maximal activity at pH 7.0, fructose reduction
5 - 7
-
at pH 5.0 and pH 7.0 about 60% of maximal activity, fructose reduction
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
45
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 50
-
50% of maximal activity at 15ĆĀ°C, 40% of maximal activity at 50ĆĀ°C
30 - 50
-
maximal activity at 30ĆĀ°C, 40% activity at 45ĆĀ°C, 30% activity at 50ĆĀ°C, no activity at 60ĆĀ°C
35 - 65
-
35ĆĀ°C: about 50% of activity maximum, 65ĆĀ°C: about 95% of activity maximum
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expression of isoform Sdh1 is elevated in high-sugar mutants, after sugar injections, and more pronounced when transfected tissues are incubated at low oxygen concentrations
-
-
brenda
isozyme SDH1; enzyme is encoded by 9 different genes encoding isozymes SDH1-SDH9
SwissProt
brenda
isozyme SDH2; enzyme is encoded by 9 different genes encoding isozymes SDH1-SDH9
SwissProt
brenda
isozyme SDH9; enzyme is encoded by 9 different genes encoding isozymes SDH1-SDH9
SwissProt
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoform Sdh1, specific for kernel and endosperm. Maximaml expression at both mRNA and enzyme activity level during early kernel development
brenda
-
enzyme activity is higher in seed than in cortex per mg and fresh weight. Isoforms SDH1 and SDH3 are expressed in both seed and cortex tissue, isoform SDH2 expression is limited to cortex
brenda
-
activity is higher than in cortex per mg and fresh weight, and contributes significantly to whole fruit activity during weeks 2-5 after bloom. Isoforms SDH1 and SDH3 are expressed in both seed and cortex tissue. Isoforms SDH6 and SDH9 are expressed in seed tissues only
brenda
-
SORD is present along the entire length of sperm flagellum, but does not show the same distribution pattern as alpha-tubulin. Sord mRNA and SORD protein expression is up-regulated during late spermiogenesis
brenda
additional information
-
electrophoretic karyotyping and array-based comparative genomic hybridization (array-CGH), comparison of four different species derived from the Saccharomyces sensu stricto complex of 22 distillery strains, overview. The genomic diversity is mainly revealed within subtelomeric regions and the losses and/or gains of fragments of chromosomes I, III, VI and IX are the most frequently observed. Statistically significant differences in the gene copy number are documented in six functional gene categories: 1. telomere maintenance via recombination, DNA helicase activity or DNA binding, 2. maltose metabolism process, glucose transmembrane transporter activity, 3. asparagine catabolism, cellular response to nitrogen starvation, localized in cell wall-bounded periplasmic space, 4. siderophore transport, 5. response to copper ion, cadmium ion binding and 6. L-iditol 2-dehydrogenase activity. Distillery yeasts are diploid. Gene ontology overrepresentation profiles are species-specific
brenda
electrophoretic karyotyping and array-based comparative genomic hybridization (array-CGH), comparison of four different species derived from the Saccharomyces sensu stricto complex of 22 distillery strains, overview. The genomic diversity is mainly revealed within subtelomeric regions and the losses and/or gains of fragments of chromosomes I, III, VI and IX are the most frequently observed. Statistically significant differences in the gene copy number are documented in six functional gene categories: 1. telomere maintenance via recombination, DNA helicase activity or DNA binding, 2. maltose metabolism process, glucose transmembrane transporter activity, 3. asparagine catabolism, cellular response to nitrogen starvation, localized in cell wall-bounded periplasmic space, 4. siderophore transport, 5. response to copper ion, cadmium ion binding and 6. L-iditol 2-dehydrogenase activity. Distillery yeasts are diploid. Gene ontology overrepresentation profiles are species-specific
brenda
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electrophoretic karyotyping and array-based comparative genomic hybridization (array-CGH), comparison of four different species derived from the Saccharomyces sensu stricto complex of 22 distillery strains, overview. The genomic diversity is mainly revealed within subtelomeric regions and the losses and/or gains of fragments of chromosomes I, III, VI and IX are the most frequently observed. Statistically significant differences in the gene copy number are documented in six functional gene categories: 1. telomere maintenance via recombination, DNA helicase activity or DNA binding, 2. maltose metabolism process, glucose transmembrane transporter activity, 3. asparagine catabolism, cellular response to nitrogen starvation, localized in cell wall-bounded periplasmic space, 4. siderophore transport, 5. response to copper ion, cadmium ion binding and 6. L-iditol 2-dehydrogenase activity. Distillery yeasts are diploid. Gene ontology overrepresentation profiles are species-specific
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electrophoretic karyotyping and array-based comparative genomic hybridization (array-CGH), comparison of four different species derived from the Saccharomyces sensu stricto complex of 22 distillery strains, overview. The genomic diversity is mainly revealed within subtelomeric regions and the losses and/or gains of fragments of chromosomes I, III, VI and IX are the most frequently observed. Statistically significant differences in the gene copy number are documented in six functional gene categories: 1. telomere maintenance via recombination, DNA helicase activity or DNA binding, 2. maltose metabolism process, glucose transmembrane transporter activity, 3. asparagine catabolism, cellular response to nitrogen starvation, localized in cell wall-bounded periplasmic space, 4. siderophore transport, 5. response to copper ion, cadmium ion binding and 6. L-iditol 2-dehydrogenase activity. Distillery yeasts are diploid. Gene ontology overrepresentation profiles are species-specific
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expression is higher at the young and mature stage than at other stages
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expression in mature leaf is higher than in young and folded leaf
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vascular tissue and mesophyll tissue of young and old leaves
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enzyme expression and activity during apple fruit set and early development, mRNA and activity is present during the first 5 wees after bloom, important for carbohydrate metabolism, overview
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enzyme expression and activity during apple fruit set and early development, mRNA and activity is present during the first 5 wees after bloom, important for carbohydrate metabolism, overview
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additional information
enzyme expression and activity during apple fruit set and early development, mRNA and activity is present during the first 5 wees after bloom, important for carbohydrate metabolism, overview
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additional information
enzyme expression and activity during apple fruit set and early development, mRNA and activityis present during the first 5 wees after bloom, important for carbohydrate metabolism, overview
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additional information
enzyme expression and activity during apple fruit set and early development, mRNA and activityis present during the first 5 wees after bloom, important for carbohydrate metabolism, overview
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additional information
enzyme expression and activity during apple fruit set and early development, mRNA and activityis present during the first 5 wees after bloom, important for carbohydrate metabolism, overview
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additional information
the enzyme is ubiquitously expressed in both sink and source organs
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the enzyme is ubiquitously expressed in both sink and source organs
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the enzyme is ubiquitously expressed in both sink and source organs
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the enzyme is ubiquitously expressed in both sink and source organs, immunohistochemic analysis, overview
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the enzyme is ubiquitously expressed in both sink and source organs, immunohistochemic analysis, overview
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additional information
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the enzyme is ubiquitously expressed in both sink and source organs, immunohistochemic analysis, overview
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sorbitol can substitute for glucose or fructose in capacitating media
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molecular karyotyping reveals the diversity of chromosome patterns, four strains with the most accented genetic variabilities are selected and subjected to genome-wide array-based comparativ genomic hybridization (array-CGH) analysis. The differences in the gene copy number are found in five functional gene categories: (1) maltose metabolism and transport, (2) response to toxin, (3) siderophore transport, (4) cellular aldehyde metabolic process, and (5) L-iditol 2-dehydrogenase activity
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additional information
molecular karyotyping reveals the diversity of chromosome patterns, four strains with the most accented genetic variabilities are selected and subjected to genome-wide array-based comparativ genomic hybridization (array-CGH) analysis. The differences in the gene copy number are found in five functional gene categories: (1) maltose metabolism and transport, (2) response to toxin, (3) siderophore transport, (4) cellular aldehyde metabolic process, and (5) L-iditol 2-dehydrogenase activity
brenda
additional information
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molecular karyotyping reveals the diversity of chromosome patterns, four strains with the most accented genetic variabilities are selected and subjected to genome-wide array-based comparativ genomic hybridization (array-CGH) analysis. The differences in the gene copy number are found in five functional gene categories: (1) maltose metabolism and transport, (2) response to toxin, (3) siderophore transport, (4) cellular aldehyde metabolic process, and (5) L-iditol 2-dehydrogenase activity
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
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SORD is associated with mitochondria and near the plasma membrane of the sperm flagellum, immunohistochemic analysis, overview
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
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sorbitol dehydrogenase can convert sorbitol to fructose, which can then be metabolized via the glycolytic pathway in sperm to make ATP. Sorbitol can serve as an alternative energy source for sperm motility and protein tyrosine phosphorylation
additional information
metabolism
NAD-SDH is a key enzyme in sorbitol metabolism and plays an important role in regulating sink strength and determining the quality of apple fruit
metabolism
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the zinc-finger protein ZAC1 is up-regulated under hypertonic stress and negatively regulates expression of SDH, allowing for accumulation of sorbitol as a compatible organic osmolyte
metabolism
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the zinc-finger protein ZAC1 is up-regulated under hypertonic stress and negatively regulates expression of SDH, allowing for accumulation of sorbitol as a compatible organic osmolyte
additional information
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comprehensive evaluation of genomic features of distillery strains, overview. Naturally occurring diversity in the YRF1 gene copy number may promote genetic stability in the Saccharomyces bayanus group of distillery yeast strains
additional information
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comprehensive evaluation of genomic features of distillery strains, overview. Naturally occurring diversity in the YRF1 gene copy number may promote genetic stability in the Saccharomyces bayanus group of distillery yeast strains
additional information
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comprehensive evaluation of genomic features of distillery strains, overview. Naturally occurring diversity in the YRF1 gene copy number may promote genetic stability in the Saccharomyces bayanus group of distillery yeast strains
additional information
comprehensive evaluation of genomic features of distillery strains, overview. Naturally occurring diversity in the YRF1 gene copy number may promote genetic stability in the Saccharomyces bayanus group of distillery yeast strains
additional information
comprehensive evaluation of genomic features of distillery strains, overview. Naturally occurring diversity in the YRF1 gene copy number may promote genetic stability in the Saccharomyces bayanus group of distillery yeast strains
Show AA Sequence and Transmembrane Helices (4486 entries)
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PDB
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CATH
UNIPROT
ORGANISM