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1,2-butanediol + NAD+
? + NADH + H+
1,2-hexanediol + NAD+
? + NADH + H+
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
3-deoxy-D-sorbitol + NAD+
? + NADH
-
-
-
-
?
3-fluoro-D-sorbitol + NAD+
3-fluoro-D-fructose + NADH + H+
-
-
-
-
r
4-deoxy-D-sorbitol + NAD+
4-deoxy-D-fructose + NADH + H+
-
-
-
-
r
4-fluoro-D-sorbitol + NAD+
4-fluoro-D-fructose + NADH + H+
-
-
-
-
r
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-adonitol + NAD+
D-ribulose + NADH
-
-
-
-
?
D-arabitol + NAD(P)+
D-xylulose + NAD(P)H + H+
D-arabitol + NAD+
D-xylulose + NADH + H+
D-fructose + NADH
?
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
D-galactitol + NAD+
D-tagatose + NADH
D-galactitol + NAD+
D-tagatose + NADH + H+
D-glucitol + NAD+
D-fructose + NADH + H+
D-gluconate + NAD+
?
-
low activity
-
-
?
D-glucose + NADH
?
-
low activity
-
-
?
D-glycero-D-gluco-heptitol + NAD+
?
-
-
-
-
?
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
D-mannitol + NAD+
D-fructose + NADH + H+
D-mannose + NADH
?
-
low activity
-
-
?
D-psicose + NADH
?
-
-
-
-
?
D-raffinose + NADH
?
-
low activity
-
-
?
D-ribose + NADH
?
-
low activity
-
-
?
D-sorbitol + 2,6-dichlorophenolindophenol
L-sorbose + ?
-
electron acceptor: i.e. DCIP
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
-
-
?
D-sorbitol + NAD(P)+
L-sorbose + NAD(P)H + H+
D-sorbitol + NAD+
? + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
D-sorbitol + NAD+
L-sorbose + NADH + H+
D-sorbose + NADH
?
-
low activity
-
-
?
D-tagatose + NADH
D-galactitol + NAD+
D-xylitol + NAD+
? + NADH + H+
D-xylitol + NADP+
? + NADPH + H+
NADP+ is not a cofactor for wild-type, but for a substrate-binding loop chimera
-
-
?
ethanol + NAD+
acetaldehyde + NADH
glycerol + NAD+
?
-
low activity
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
L-erythrulose + NADH
?
-
-
-
-
?
L-rhamnose + NADH
?
-
low activity
-
-
?
meso-erythritol + NAD+
erythrulose + NADH
-
high activity
-
-
?
ribitol + NAD+
?
60% of the activity with D-sorbitol
-
-
?
sorbitol + NAD+
D-fructose + NADH
Xylitol + NAD+
?
29% of the activity with D-sorbitol
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
additional information
?
-
1,2-butanediol + NAD+
? + NADH + H+
-
-
-
?
1,2-butanediol + NAD+
? + NADH + H+
-
-
-
?
1,2-hexanediol + NAD+
? + NADH + H+
-
-
-
?
1,2-hexanediol + NAD+
? + NADH + H+
-
-
-
?
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-arabinose + NADH
?
-
low activity
-
-
?
D-arabinose + NADH
?
-
low activity
-
-
?
D-arabitol + NAD(P)+
D-xylulose + NAD(P)H + H+
-
-
-
?
D-arabitol + NAD(P)+
D-xylulose + NAD(P)H + H+
-
-
-
?
D-arabitol + NAD+
?
-
D-arabinitol is identical, low activity
-
-
?
D-arabitol + NAD+
?
Cereibacter sphaeroides Si4 / DSM 8371
-
D-arabinitol is identical, low activity
-
-
?
D-arabitol + NAD+
?
-
D-arabinitol is identical, low activity
-
-
?
D-arabitol + NAD+
?
-
D-arabinitol is identical, low activity
-
-
?
D-arabitol + NAD+
?
-
D-arabinitol is identical, low activity
-
-
?
D-arabitol + NAD+
?
-
D-arabinitol is identical, low activity
-
-
?
D-arabitol + NAD+
D-xylulose + NADH + H+
-
best substrate
-
-
?
D-arabitol + NAD+
D-xylulose + NADH + H+
-
best substrate
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
r
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-galactitol + NAD+
D-tagatose + NADH
-
-
-
-
?
D-galactitol + NAD+
D-tagatose + NADH
-
-
-
r
D-galactitol + NAD+
D-tagatose + NADH
-
low activity
-
-
?
D-galactitol + NAD+
D-tagatose + NADH
-
-
-
r
D-galactitol + NAD+
D-tagatose + NADH
-
-
-
-
?
D-galactitol + NAD+
D-tagatose + NADH + H+
-
-
-
?
D-galactitol + NAD+
D-tagatose + NADH + H+
-
-
-
?
D-glucitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-glucitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
-
-
-
?
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
-
-
-
?
D-mannitol + NAD+
?
-
low activity
-
-
?
D-mannitol + NAD+
?
-
low activity
-
-
?
D-mannitol + NAD+
?
-
low activity
-
-
?
D-mannitol + NAD+
?
-
low activity
-
-
?
D-mannitol + NAD+
?
-
-
-
-
?
D-mannitol + NAD+
?
-
low activity
-
-
?
D-mannitol + NAD+
?
-
low activity
-
-
?
D-mannitol + NAD+
?
-
-
-
-
?
D-mannitol + NAD+
?
-
-
-
-
?
D-mannitol + NAD+
?
-
low activity
-
-
?
D-mannitol + NAD+
?
-
-
-
-
?
D-mannitol + NAD+
?
-
low activity
-
-
?
D-mannitol + NAD+
?
6% of the activity with D-sorbitol
-
-
?
D-mannitol + NAD+
?
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-ribitol + NAD+
?
-
-
-
-
?
D-ribitol + NAD+
?
-
-
-
-
?
D-ribitol + NAD+
?
-
-
-
-
?
D-ribitol + NAD+
?
-
-
-
-
?
D-ribitol + NAD+
?
-
-
-
-
?
D-ribitol + NAD+
?
-
-
-
-
?
D-ribitol + NAD+
?
-
-
-
-
?
D-ribitol + NAD+
?
-
-
-
-
?
D-ribitol + NAD+
?
-
-
-
-
?
D-ribitol + NAD+
?
-
-
-
-
?
D-ribulose + NADH
?
-
-
-
-
?
D-ribulose + NADH
?
-
-
-
-
?
D-ribulose + NADH
?
-
-
-
-
?
D-ribulose + NADH
?
-
-
-
-
?
D-ribulose + NADH
?
-
-
-
-
?
D-sorbitol + NAD(P)+
L-sorbose + NAD(P)H + H+
-
-
-
?
D-sorbitol + NAD(P)+
L-sorbose + NAD(P)H + H+
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
Cereibacter sphaeroides Si4 / DSM 8371
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + 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+
-
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
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+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
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, 2- and 4-hydroxy groups of D-sorbitol are important for substrate bindig
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
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+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
part of the polyol pathway that interconverts glucose and fructose
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
?
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
-
-
?
D-tagatose + NADH
D-galactitol + NAD+
-
-
-
-
r
D-tagatose + NADH
D-galactitol + NAD+
-
-
-
-
?
D-tagatose + NADH
D-galactitol + NAD+
-
-
-
-
r
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
low activity
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
low activity
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
?
-
-
-
-
?
D-xylitol + NAD+
? + NADH + H+
-
-
-
?
D-xylitol + NAD+
? + NADH + H+
-
-
-
?
D-xylose + NADH
?
-
low activity
-
-
?
D-xylose + NADH
?
-
low activity
-
-
?
D-xylulose + NADH
?
-
low activity
-
-
?
D-xylulose + NADH
?
Cereibacter sphaeroides Si4 / DSM 8371
-
low activity
-
-
?
D-xylulose + NADH
?
-
-
-
-
?
D-xylulose + NADH
?
-
-
-
-
?
D-xylulose + NADH
?
-
-
-
-
?
D-xylulose + NADH
?
-
-
-
-
?
D-xylulose + NADH
?
-
low activity
-
-
?
D-xylulose + NADH
?
-
-
-
-
?
D-xylulose + NADH
?
-
-
-
-
?
erythritol + NAD+
?
-
low activity
-
-
?
erythritol + NAD+
?
-
-
-
-
?
erythritol + NAD+
?
13% of the activity with D-sorbitol
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
low activity
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
L-arabitol + NAD+
?
-
-
-
-
?
L-arabitol + NAD+
?
-
-
-
-
?
L-arabitol + NAD+
?
Cereibacter sphaeroides Si4 / DSM 8371
-
-
-
-
?
L-arabitol + NAD+
?
-
low activity
-
-
?
L-arabitol + NAD+
?
-
-
-
-
?
L-arabitol + NAD+
?
-
low activity
-
-
?
L-arabitol + NAD+
?
-
-
-
-
?
L-arabitol + NAD+
?
-
low activity
-
-
?
L-arabitol + NAD+
?
-
-
-
-
?
L-arabitol + NAD+
?
13% of the activity with D-sorbitol
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
Cereibacter sphaeroides Si4 / DSM 8371
-
-
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
-
-
-
-
?
L-iditol + NAD+
?
79% of the activity with D-sorbitol
-
-
?
L-iditol + NAD+
?
-
low activity
-
-
?
L-sorbose + NADH
?
-
-
-
-
?
L-sorbose + NADH
?
-
low activity
-
-
?
L-sorbose + NADH
?
-
-
-
-
?
L-sorbose + NADH
?
-
-
-
-
?
L-sorbose + NADH
?
-
-
-
-
?
L-sorbose + NADH
?
-
low activity
-
-
?
L-sorbose + NADH
?
-
-
-
-
?
L-sorbose + NADH
?
-
-
-
-
?
L-sorbose + NADH
?
-
low activity
-
-
?
L-threitol + NAD+
?
-
low activity
-
-
?
L-threitol + NAD+
?
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-
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-
?
L-threitol + NAD+
?
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-
?
sorbitol + NAD+
D-fructose + NADH
-
-
-
r
sorbitol + NAD+
D-fructose + NADH
-
-
-
-
?
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
?
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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
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-
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additional information
?
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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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isoform Sdh1, specific for kernel and endosperm
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cell culture derived from the kidney inner medulla
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isoform Sdh1, specific for kernel and endosperm. Maximaml expression at both mRNA and enzyme activity level during early kernel development
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tissue culture
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ventral and dorsal
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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
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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
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shoot tip
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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
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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
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
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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expression is higher at the young and mature stage than at other stages
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sorbitol dehydrogenase is active throughout development
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flesh and vascular tissue
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papilla, inner medulla, cortex
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papilla, inner medulla, cortex
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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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285872, 285880, 285883, 285889, 285891, 285893, 285894, 285900, 655289, 684974, 687821 brenda
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commercial preparation
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additional information
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SDH expression analysis, 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 activity is present during the first 5 wees after bloom, important for carbohydrate metabolism, overview
brenda
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
brenda
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
brenda
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
brenda
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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additional information
the enzyme is ubiquitously expressed in both sink and source organs
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additional information
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the enzyme is ubiquitously expressed in both sink and source organs
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additional information
the enzyme is ubiquitously expressed in both sink and source organs, immunohistochemic analysis, overview
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additional information
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
brenda
additional information
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SDH expression analysis, overview
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additional information
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sorbitol can substitute for glucose or fructose in capacitating media
brenda
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
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
-
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
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DNA and amino acid sequence determination and analysis, co-expression with gene sldB in Escherichia coli strain JM109, sldB and PQQ are required for recombinant activity in Escherichia coli, co-expression of sldB is also required for enzyme activity in vivo
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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
expressed in Pseudomonas putida strain IFO3738 fused to 6 x His-tag
expression in Escherichia coli
expression in Escherichia coli strain BL21
-
expression of wild-type and mutant enzymes in Escherichia coli
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gene GoSCR, recombinant expression of His-tagged enzyme GoSCR in Escherichia coli strain BL21 (DE3), coexpression with 2,3-butanediol dehydrogenase (BDHA) from Bacillus subtilis for asymmetric reduction of 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) or (S)-1-phenyl-1,2-ethanediol ((S)-PED)
gene MdSDH5, DNA and amino acid sequence determination and analysis, transient expression of MdSDH5-GFP and MdSDH6-GFP in the mesophyll protoplast of Arabidopsis thaliana
gene MdSDH6, DNA and amino acid sequence determination and analysis, phylogenetic tree, transient expression of MdSDH5-GFP and MdSDH6-GFP in the mesophyll protoplast of Arabidopsis thaliana
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
-
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. Genomic stability and nucleolus state are affected in Saflager W-34/70 strain
multiple genes, DNA sequence determination and analysis, a cDNA is expressed in Escherichia coli
-
-
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
-
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
-
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
-
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
expression in Escherichia coli
-
expression in Escherichia coli
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Leissing, N.; McGuinness, E.T.
Sorbitol dehydrogenase from rat liver
Methods Enzymol.
89
135-140
1982
Ovis aries, Rattus norvegicus
brenda
Jeffery, J.; Cummins, L.; Carlquist, M.; Jrnvall, H.
Properties of sorbitol dehydrogenase and characterization of a reactive cysteine residue reveal unexpected similarities to alcohol dehydrogenases
Eur. J. Biochem.
120
229-234
1981
Ovis aries
brenda
Negm, F.B.; Loescher, W.H.
Detection and characterization of sorbitol dehydrogenase from apple callus tissue
Plant Physiol.
64
69-73
1979
Malus domestica
brenda
Dooley, J.F.; Turnquist, L.J.; Racich, L.
Kinetic determination of serum sorbitol dehydrogenase activity with a centrifugal analyzer
Clin. Chem.
25
2026-2029
1979
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Leissing, N.; Mc Guinness, E.T.
Rapid affinity purification and properties of rat liver sorbitol dehydrogenase
Biochim. Biophys. Acta
524
254-261
1978
Rattus norvegicus
brenda
Gerlach, U.; Hiby, W.
Sorbit-Dehydrogenase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
601-606
1974
Homo sapiens, Rattus norvegicus
-
brenda
Myers, J.S.; Jakoby, W.B.
Effect of polyhydric alcohols on kinetic parameters of enzymes
Biochem. Biophys. Res. Commun.
51
631-636
1973
Ovis aries
brenda
Rehg, J.E.; Torack, R.M.
Partial purification and characterization of sorbitol dehydrogenase from rat brain
J. Neurochem.
28
655-660
1977
Rattus norvegicus
brenda
Smith, M.G.
Polyol dehydrogenase
Biochem. J.
83
135-144
1962
Ovis aries
brenda
Williams-Ashman, H.G.; Banks, J.; Wolfson, S.K.
Oxidation of polyhydric alcohols by the prostate gland and seminal vesicle
Arch. Biochem. Biophys.
72
485-494
1957
Rattus norvegicus
brenda
King, T.E.; Mann, T.
Sorbitol metabolism in spermatozoa
Proc. R. Soc. Lond. B Biol. Sci.
151
226-243
1959
Cavia porcellus, Ovis aries
-
brenda
Bailey, J.P.; Renz, C.; McGuinness, E.T.
Sorbitol dehydrogenase from horse liver: Purification, characterization and comparative properties
Comp. Biochem. Physiol. B
69
909-914
1981
Equus caballus, Ovis aries
-
brenda
Rizzi, M.; Harwart, K.; Erlemann, P.; Bui-Thanh, N.A.; Dellweg, H.
Purification and properties of the NAD+-xylitol-dehydrogenase from the yeast Pichia stipitis
J. Ferment. Bioeng.
67
20-24
1989
Scheffersomyces stipitis
-
brenda
Rizzi, M.; Harwart, K.; Bui-Thanh, N.A.; Dellweg, H.
A kinetic study of the NAD+-xylitol-dehydrogenase from the yeast Pichia stipitis
J. Ferment. Bioeng.
67
25-30
1989
Scheffersomyces stipitis
-
brenda
Schneider, K.H.; Giffhorn, F.
Sorbitol dehydrogenase from Pseudomonas sp.: Purification, characterization and application to quantitative determination of sorbitol
Enzyme Microb. Technol.
13
332-337
1991
Pseudomonas sp.
-
brenda
Ng, K.; Ye, R.; Wu, X.C.; Wong, S.L.
Sorbitol dehydrogenase from Bacillus subtilis, purification, characterization and gene cloning
J. Biol. Chem.
267
24989-24994
1992
Bacillus subtilis
brenda
Yamaguchi, H.; Kanayama, Y.; Yamaki, S.
Purification and properties of NAD-dependent sorbitol dehydrogenase from apple fruit
Plant Cell Physiol.
35
887-892
1994
Malus domestica
-
brenda
Lindstad, R.I.; Hermansen, L.F.; McKinley-McKee, J.S.
Inhibition and activation studies on sheep liver sorbitol dehydrogenase
Eur. J. Biochem.
221
847-854
1994
Ovis aries
brenda
Schauder, S.; Schneider, K.H.; Giffhorn, F.
Polyol metabolism of Rhodobacter sphaeroides: biochemical characterization of a short-chain sorbitol dehydrogenase
Microbiology
141
1857-1863
1995
Cereibacter sphaeroides, Cereibacter sphaeroides Si4 / DSM 8371
brenda
Lindstad, R.I.; McKinley-McKee, J.S.
Effect of pH on sheep liver sorbitol dehydrogenase steady-state kinetics
Eur. J. Biochem.
233
891-898
1995
Ovis aries
brenda
Maret, W.
Human sorbitol dehydrogenase - a secondary alcohol dehydrogenase with distinct pathophysiological roles, pH dependent kinetic studies
Adv. Exp. Med. Biol.
383-393
1996
Homo sapiens
brenda
Kvernmo, T.; Winberg, J.O.; McKinley-McKee, J.S.
Reversible and irreversible inhibition of sheep liver sorbitol dehydrogenase with Cibaron Blue 3GA and Eriochrome Black T
Int. J. Biochem. Cell Biol.
28
303-309
1996
Ovis aries
brenda
Lindstad, R.I.; McKinley-McKee, J.S.
Reversible inhibition of sheep liver sorbitol dehydrogenase by thiol compounds
Eur. J. Biochem.
241
142-148
1996
Ovis aries
brenda
Marini, I.; Bucchioni, L.; Borella, P.; Del Corso, A.; Mura, U.
Sorbitol dehydrogenase from bovine lens: purification and properties
Arch. Biochem. Biophys.
340
383-391
1997
Bos taurus
brenda
Takayuki, U.
Purification and properties of NAD+-dependent sorbitol dehydrogenase from Bacillus fructosus
Biosci. Biotechnol. Biochem.
63
573-574
1999
Priestia megaterium
brenda
Adachi, O.; Toyama, H.; Theeragool, G.; Lotong, N.; Matsushita, K.
Crystallization and properties of NAD-dependent D-sorbitol dehydrogenase from Gluconobacter suboxydans IFO 3257
Biosci. Biotechnol. Biochem.
63
1589-1595
1999
Gluconobacter oxydans, Gluconobacter oxydans IFO3257
brenda
Marini, I.; Moschini, R.; Del Corso, A.; Mura, U.
Complete protection by alpha-crystallin of lens sorbitol dehydrogenase undergoing thermal stress
J. Biol. Chem.
275
32559-32565
2000
Bos taurus
brenda
Oura, Y.; Yamada, K.; Shiratake, K.; Yamaki, S.
Purification and characterization of NAD+-dependent sorbitol dehydrogenase from Japanese pear fruit
Phytochemistry
54
567-572
2000
Pyrus pyrifolia
brenda
Boguslawski, G.; Bertch, S.W.
A method for the assay of glucose isomerase activity in complex fermentation mixtures
J. Appl. Biochem.
2
367-372
1980
Ovis aries
-
brenda
Vongsuvanlert, V.; Tani, Y.
Characterization of D-sorbitol dehydrogenase involved in D-sorbitol production of a methanol yeast, Candida boidinii (Kloeckera sp.) No. 2201
Agric. Biol. Chem.
52
419-426
1988
[Candida] boidinii
-
brenda
Darmanin, C.; Iwata, T.; Carper, D.A.; Sparrow, L.G.; Chung, R.P.; El-Kabbani, O.
Expression, purification and preliminary crystallographic analysis of human sorbitol dehydrogenase
Acta Crystallogr. Sect. D
59
558-560
2003
Homo sapiens
brenda
Hoshino, T.; Sugisawa, T.; Shinjoh, M.; Tomiyama, N.; Miyazaki, T.
Membrane-bound D-sorbitol dehydrogenase of Gluconobacter suboxydans IFO 3255 - enzymatic and genetic characterization
Biochim. Biophys. Acta
1647
278-288
2003
Gluconobacter oxydans, Gluconobacter oxydans IFO 3255
brenda
Shinjoh, M.; Tomiyama, N.; Miyazaki, T.; Hoshino, T.
Main polyol dehydrogenase of Gluconobacter suboxydans IFO 3255, membrane-bound D-sorbitol dehydrogenase, that needs product of upstream gene, sldB, for activity
Biosci. Biotechnol. Biochem.
66
2314-2322
2002
Gluconobacter oxydans, Gluconobacter oxydans IFO 3255
brenda
Sugisawa, T.; Hoshino, T.
Purification and properties of membrane-bound D-sorbitol dehydrogenase from Gluconobacter suboxydans IFO 3255
Biosci. Biotechnol. Biochem.
66
57-64
2002
Gluconobacter oxydans, Gluconobacter oxydans IFO 3255
brenda
El-Kabbani, O.; Darmanin, C.; Chung, R.P.
Sorbitol dehydrogenase: structure, function and ligand design
Curr. Med. Chem.
11
465-476
2004
Ovis aries, Homo sapiens, Mammalia, Rattus norvegicus
brenda
Parmentier, S.; Arnaut, F.; Vandamme, E.J.
Gluconobacter NAD-dependent polyol dehydrogenase catalyzed production of D-sorbitol and D-mannitol with coenzyme regeneration
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Homo sapiens (Q00796), Homo sapiens
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Philippsen, A.; Schirmer, T.; Stein, M.A.; Giffhorn, F.; Stetefeld, J.
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Cereibacter sphaeroides
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Marini, I.; Moschini, R.; Del Corso, A.; Mura, U.
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Bos taurus
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Solanum lycopersicum (Q3C2L6), Solanum lycopersicum
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Shibata, T.; Ichikawa, C.; Matsuura, M.; Takata, Y.; Noguchi, Y.; Saito, Y.; Yamashita, M.
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Klimacek, M.; Hellmer, H.; Nidetzky, B.
Catalytic mechanism of Zn2+-dependent polyol dehydrogenases: kinetic comparison of sheep liver sorbitol dehydrogenase with wild-type and Glu154-Cys forms of yeast xylitol dehydrogenase
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Hellgren, M.; Kaiser, C.; de Haij, S.; Norberg, A.; Hoeoeg, J.O.
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Malus domestica
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Fragaria x ananassa
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de Sousa, S.M.; Paniago, M.D.; Arruda, P.; Yunes, J.A.
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Zea mays
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Cao, W.; Aghajanian, H.; Haig-Ladewig, L.; Gerton, G.
Sorbitol can fuel mouse sperm motility and protein tyrosine phosphorylation via sorbitol dehydrogenase
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Mus musculus
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Lanaspa, M.A.; Andres-Hernando, A.; Rivard, C.J.; Dai, Y.; Li, N.; Berl, T.
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Homo sapiens, Mus musculus
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Wang, X.L.; Xu, Y.H.; Peng, C.C.; Fan, R.C.; Gao, X.Q.
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Malus domestica (Q5I6M3), Malus domestica (Q5I6M4), Malus domestica
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Landau, Z.; Novotny, M.J.; Preston, G.M.; Wright, K.; Freeman, T.; Dai, H.; Thompson, J.; Oates, P.J.; Calle, R.A.
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Deinococcus geothermalis (Q1J2J0), Deinococcus geothermalis, Deinococcus geothermalis DSM 11300 (Q1J2J0)
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Selvaraj, C.; Krishnasamy, G.; Jagtap, S.; Patel, S.; Dhiman, S.; Kim, T.; Singh, S.; Lee, J.
Structural insights into the binding mode of D-sorbitol with sorbitol dehydrogenase using QM-polarized ligand docking and molecular dynamics simulations
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Gluconobacter oxydans (Q9KWR5)
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Adamczyk, J.; Deregowska, A.; Skoneczny, M.; Skoneczna, A.; Natkanska, U.; Kwiatkowska, A.; Rawska, E.; Potocki, L.; Kuna, E.; Panek, A.; Lewinska, A.; Wnuk, M.
Copy number variations of genes involved in stress responses reflect the redox state and DNA damage in brewing yeasts
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Saccharomyces cerevisiae (P35497), Saccharomyces cerevisiae (Q07786), Saccharomyces cerevisiae
brenda
Deregowska, A.; Skoneczny, M.; Adamczyk, J.; Kwiatkowska, A.; Rawska, E.; Skoneczna, A.; Lewinska, A.; Wnuk, M.
Genome-wide array-CGH analysis reveals YRF1 gene copy number variation that modulates genetic stability in distillery yeasts
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Saccharomyces bayanus, Saccharomyces paradoxus, Saccharomyces kudriavzevii, Saccharomyces cerevisiae (P35497), Saccharomyces cerevisiae (Q07786)
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Periyasamy, S.; Govindappa, N.; Sreenivas, S.; Sastry, K.
Isolation, characterization and evaluation of the Pichia pastoris sorbitol dehydrogenase promoter for expression of heterologous proteins
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Komagataella pastoris, Komagataella pastoris BICC 9450
brenda
Cui, Z.; Zhang, J.; Fan, X.; Zheng, G.; Chang, H.; Wei, W.
Highly efficient bioreduction of 2-hydroxyacetophenone to (S)- and (R)-1-phenyl-1,2-ethanediol by two substrate tolerance carbonyl reductases with cofactor regeneration
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Gluconobacter oxydans (Q5FNX9), Gluconobacter oxydans 621H (Q5FNX9)
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Dong, F.; Wang, C.; Sun, X.; Bao, Z.; Dong, C.; Sun, C.; Ren, Y.; Liu, S.
Sugar metabolic changes in protein expression associated with different light quality combinations in tomato fruit
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Solanum lycopersicum (Q3C2L6)
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brenda