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1,4-dibromo-2,3-butanedione + NAD(P)H
? + NAD(P)+
1,4-dibromo-2,3-butanedione + NADPH
? + NADP+
-
dicarbonyl reductase activity
-
-
r
D-erythrose + NADPH + H+
? + NADP+
-
-
-
ir
D-fructose + NADPH + H+
? + NADP+
low activity
-
-
?
D-ribulose + NADH
D-arabinitol + NAD+
-
-
-
r
D-ribulose + NADPH
D-ribitol + NADP+
D-ribulose + NADPH + H+
? + NADP+
-
-
-
?
D-ribulose + NADPH + H+
D-ribitol + NADP+
-
-
-
-
?
D-sorbitol + NADP+
?
-
-
-
-
?
D-sorbitol + NADP+
D-sorbose + NADPH + H+
D-threose + NADPH
D-threitol + NADP+
D-threose + NADPH + H+
? + NADP+
-
-
-
ir
D-xylulose + NADH + H+
D-arabinitol + NAD+
D-xylulose + NADPH + H+
D-xylitol + NADP+
D-xylulose + NADPH + H+
xylitol + NADP+
diacetyl + NAD(P)H
acetoin + NAD(P)+
diacetyl + NADPH + H+
acetoin + NADP+
-
-
-
?
DL-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
DL-threitol + NAD+
D-threose + NADH
DL-threitol + NADP+
D-erythrulose + NADPH
-
probably identical with erythrulose reductase, EC 1.1.1.162 and diacetyl reductase, EC 1.1.1.5
-
r
L-erythrulose + NADPH + H+
? + NADP+
-
-
-
ir
L-ribulose + NADPH + H+
? + NADP+
low activity
-
-
?
L-sorbose + NADPH + H+
L-sorbitol + NADP+
L-threose + NADPH
L-threitol + NADP+
L-xylulose + NADH
L-xylitol + NAD+
L-xylulose + NADH + H+
xylitol + NAD+
L-xylulose + NADPH + H+
L-xylitol + NADP+
L-xylulose + NADPH + H+
xylitol + NADP+
xylitol + NAD+
L-xylulose + NADH + H+
xylitol + NADP+
L-xylulose + NADPH + H+
xylitol + NADP+
xylulose + NADPH + H+
-
-
-
?
additional information
?
-
1,4-dibromo-2,3-butanedione + NAD(P)H
? + NAD(P)+
dicarbonyl reductase activity, best substrate, NADPH is the preferred cofactor, forward reaction is preferred
-
-
r
1,4-dibromo-2,3-butanedione + NAD(P)H
? + NAD(P)+
dicarbonyl reductase activity, best substrate, NADPH is the preferred cofactor, forward reaction is preferred
-
-
r
1,4-dibromo-2,3-butanedione + NAD(P)H
? + NAD(P)+
dicarbonyl reductase activity, best substrate, NADPH is the preferred cofactor, forward reaction is preferred
-
-
r
1,4-dibromo-2,3-butanedione + NAD(P)H
? + NAD(P)+
dicarbonyl reductase activity, best substrate, NADPH is the preferred cofactor, forward reaction is preferred
-
-
r
1,4-dibromo-2,3-butanedione + NAD(P)H
? + NAD(P)+
dicarbonyl reductase activity, best substrate, NADPH is the preferred cofactor, forward reaction is preferred
-
-
r
D-erythrose + NADPH
?
reductase activity
-
-
r
D-erythrose + NADPH
?
reductase activity
-
-
r
D-erythrose + NADPH
?
reductase activity
-
-
r
D-erythrose + NADPH
?
reductase activity
-
-
r
D-erythrose + NADPH
?
reductase activity
-
-
r
D-ribulose + NADPH
D-ribitol + NADP+
reductase activity
-
-
r
D-ribulose + NADPH
D-ribitol + NADP+
reductase activity
-
-
r
D-ribulose + NADPH
D-ribitol + NADP+
reductase activity
-
-
r
D-ribulose + NADPH
D-ribitol + NADP+
reductase activity
-
-
r
D-ribulose + NADPH
D-ribitol + NADP+
-
-
-
-
?
D-ribulose + NADPH
D-ribitol + NADP+
reductase activity
-
-
r
D-sorbitol + NADP+
D-sorbose + NADPH + H+
-
-
-
?
D-sorbitol + NADP+
D-sorbose + NADPH + H+
-
-
-
?
D-threose + NADPH
D-threitol + NADP+
reductase activity
-
-
r
D-threose + NADPH
D-threitol + NADP+
reductase activity
-
-
r
D-threose + NADPH
D-threitol + NADP+
reductase activity
-
-
r
D-threose + NADPH
D-threitol + NADP+
reductase activity
-
-
r
D-threose + NADPH
D-threitol + NADP+
reductase activity
-
-
r
D-xylulose + NADH + H+
D-arabinitol + NAD+
about 100fold lower activity compared to L-xylulose
-
-
r
D-xylulose + NADH + H+
D-arabinitol + NAD+
-
-
-
?
D-xylulose + NADPH + H+
D-xylitol + NADP+
reductase activity
-
-
r
D-xylulose + NADPH + H+
D-xylitol + NADP+
reductase activity
-
-
r
D-xylulose + NADPH + H+
D-xylitol + NADP+
reductase activity
-
-
r
D-xylulose + NADPH + H+
D-xylitol + NADP+
reductase activity
-
-
r
D-xylulose + NADPH + H+
D-xylitol + NADP+
reductase activity
-
-
r
D-xylulose + NADPH + H+
xylitol + NADP+
-
-
-
?
D-xylulose + NADPH + H+
xylitol + NADP+
low activity
-
-
?
diacetyl + NAD(P)H
acetoin + NAD(P)+
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
-
dicarbonyl reductase activity
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
dicarbonyl reductase activity
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
-
-
-
?
diacetyl + NAD(P)H
acetoin + NAD(P)+
-
dicarbonyl reductase activity
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
-
-
-
?
diacetyl + NAD(P)H
acetoin + NAD(P)+
-
detoxification of alpha-dicarbonyl compounds
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
-
dicarbonyl reductase activity
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
-
r
DL-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
reductase activity, forward reaction is highly preferred
-
-
r
DL-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
reductase activity, forward reaction is highly preferred
-
-
r
DL-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
reductase activity, forward reaction is highly preferred
-
-
r
DL-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
reductase activity, forward reaction is highly preferred
-
-
r
DL-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
reductase activity, forward reaction is highly preferred
-
-
r
DL-threitol + NAD+
D-threose + NADH
-
-
-
?
DL-threitol + NAD+
D-threose + NADH
-
-
-
?
DL-threitol + NAD+
D-threose + NADH
-
-
-
?
DL-threitol + NAD+
D-threose + NADH
-
-
-
r
L-erythrulose + NADPH
?
reductase activity
-
-
r
L-erythrulose + NADPH
?
reductase activity
-
-
r
L-erythrulose + NADPH
?
reductase activity
-
-
r
L-erythrulose + NADPH
?
reductase activity
-
-
r
L-erythrulose + NADPH
?
reductase activity
-
-
r
L-sorbose + NADPH + H+
L-sorbitol + NADP+
low activity
-
-
?
L-sorbose + NADPH + H+
L-sorbitol + NADP+
low activity
-
-
?
L-threose + NADPH
L-threitol + NADP+
reductase activity
-
-
r
L-threose + NADPH
L-threitol + NADP+
reductase activity
-
-
r
L-threose + NADPH
L-threitol + NADP+
reductase activity
-
-
r
L-threose + NADPH
L-threitol + NADP+
reductase activity
-
-
r
L-threose + NADPH
L-threitol + NADP+
reductase activity
-
-
r
L-xylulose + NADH
L-xylitol + NAD+
-
-
-
r
L-xylulose + NADH
L-xylitol + NAD+
part of the L-arabinose catabolism
-
-
r
L-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
L-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
L-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
L-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
reductase activity
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
also reduces 2,3-butadione
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
part of the glucuronic acid pathway, enzyme may be involved in water reabsorption and cellular osmoregulation
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
the enzyme is involved in the uronate cycle of glucose metabolism
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
L-xylulose reductase activity
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
reductase activity
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
uronate cycle of glucose metabolism
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
reductase activity
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
reductase activity
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
uronate cycle of glucose metabolism
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
part of the uronate cycle, involved in osmoregulation in the kidney
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
L-xylulose reductase activity
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
reductase activity
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
uronate cycle of glucose metabolism
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
xylulose reductase has about 50% higher activity during xylose consumption than during the coconsumption of glucose and xylose
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
uronate cycle of glucose metabolism
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
-
-
-
-
?
L-xylulose + NADPH + H+
xylitol + NADP+
-
-
-
ir
L-xylulose + NADPH + H+
xylitol + NADP+
-
-
-
r
L-xylulose + NADPH + H+
xylitol + NADP+
preferred substrate
-
-
r
L-xylulose + NADPH + H+
xylitol + NADP+
preferred substrate
-
-
r
xylitol + NAD+
L-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
L-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
L-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
L-xylulose + NADH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
-
?
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
-
?
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
?
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
?
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
strain DM101 and DM122, product identification is not exact, could also be D-xylulose
?
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
?
xylitol + NADP+
L-xylulose + NADPH + H+
-
engineered enzyme with altered cofactor specificity
-
-
?
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
-
-
-
r
additional information
?
-
NADH-linked enzyme form, no activity with NADPH and NADP+, no activity with L-arabinitol, adonitol or ribitol, dulcitol or galactitol, D-mannitol, and D-sorbitol, no activity with D-sorbose, L-sorbose, D-psicose, and D-fructose
-
-
?
additional information
?
-
-
NADH-linked enzyme form, no activity with NADPH and NADP+, no activity with L-arabinitol, adonitol or ribitol, dulcitol or galactitol, D-mannitol, and D-sorbitol, no activity with D-sorbose, L-sorbose, D-psicose, and D-fructose
-
-
?
additional information
?
-
-
minimal reductive activity also with D-xylulose, D-erythrose and dihydroxyacetone
-
-
?
additional information
?
-
-
no substrate: D-fructose, D-sorbose, L-sorbose, xylitol, D-arabitol, L-arabitol, ribitol, D-sorbitol and galactitol
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
dicarbonyl/L-xylulose reductase is bifunctional
-
-
?
additional information
?
-
-
dicarbonyl/L-xylulose reductase is bifunctional
-
-
?
additional information
?
-
-
no activity in the mitochondrial fraction with D-xylulose, D-sorbose, L-sorbose, L-erythrulose, D-fructose, D-sorbitol, L-arabitol, D-gulitol, D-talitol
-
-
?
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
?
additional information
?
-
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
?
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
?
additional information
?
-
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
?
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
?
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
?
additional information
?
-
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
?
additional information
?
-
-
minimal oxidative activity with D-arabitol, mannitol, 1,2-propanediol and 2,3-butanediol
-
-
?
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
?
additional information
?
-
-
the size and hydrophobicity of the amino acid residues involved in substrate recognition, i.e. Q137, L143, H146, N190, and W191, is important, mutants N190V, N190V/W191S, Q137M/L143F/H146L, and N190V/W191S/Q137M/L143F/H146L show reductive activity with 4-nitroacetophenone, 5beta-androstane-3,17-dione, 5beta-androstan-17beta-ol-3-one, and 5beta-androstane-3alpha,17beta-diol, overview
-
-
?
additional information
?
-
substrate specificity in oxidation and reduction reactions, overview. No activity with D-mannitol, D-sorbitol, D-xylose, or D-fructose as substrates. D-Xylulose is a poor substrate. Enzyme RpLXR exhibits not only a L-xylulose reductase activity but also a strong dicarbonyl reductase activity
-
-
-
additional information
?
-
-
substrate specificity in oxidation and reduction reactions, overview. No activity with D-mannitol, D-sorbitol, D-xylose, or D-fructose as substrates. D-Xylulose is a poor substrate. Enzyme RpLXR exhibits not only a L-xylulose reductase activity but also a strong dicarbonyl reductase activity
-
-
-
additional information
?
-
substrate specificity in oxidation and reduction reactions, overview. No activity with D-mannitol, D-sorbitol, D-xylose, or D-fructose as substrates. D-Xylulose is a poor substrate. Enzyme RpLXR exhibits not only a L-xylulose reductase activity but also a strong dicarbonyl reductase activity
-
-
-
additional information
?
-
-
substrate specificity in oxidation and reduction reactions, overview. No activity with D-mannitol, D-sorbitol, D-xylose, or D-fructose as substrates. D-Xylulose is a poor substrate. Enzyme RpLXR exhibits not only a L-xylulose reductase activity but also a strong dicarbonyl reductase activity
-
-
-
additional information
?
-
substrate specificity, overview. No activity with L-xylo-3-hexulose, D-sorbose, D-ribitol, D-arabitol, or L-arabitol
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with L-xylo-3-hexulose, D-sorbose, D-ribitol, D-arabitol, or L-arabitol
-
-
?
additional information
?
-
substrate specificity, overview. No activity with L-xylo-3-hexulose, D-sorbose, D-ribitol, D-arabitol, or L-arabitol
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.005 - 0.139
1,4-dibromo-2,3-butanedione
2.7
D-arabinitol
pH 9.0, 30°C, purified recombinant enzyme
250
D-sorbitol
pH 7.0, 30°C, recombinant enzyme
1.6 - 60
dihydroxyacetone
1.2 - 6
DL-glyceraldehyde
0.18
L-ribulose
pH 7.0, temperature not specified in the publication
0.005
1,4-dibromo-2,3-butanedione
-
pH 7.0, 25°C, wild-type enzyme
0.05
1,4-dibromo-2,3-butanedione
-
pH 7.0, 25°C, mutant S136A
0.1
1,4-dibromo-2,3-butanedione
-
pH 7.0, 25°C, mutant K153M
0.139
1,4-dibromo-2,3-butanedione
-
pH 7.0, 25°C, mutant Y149F
1.5
acetoin
pH 7.0, 25°C
0.27
D-erythrose
pH 7.0, temperature not specified in the publication
0.59
D-erythrose
pH 7.0, 25°C
2.4
D-erythrose
pH 7.0, 25°C
3.9
D-erythrose
pH 7.0, 25°C
5.7
D-erythrose
pH 7.0, 25°C
6
D-erythrose
pH 7.0, 25°C
4.7
D-ribulose
pH 7.0, 30°C, purified recombinant enzyme
5
D-ribulose
pH 7.0, 25°C
5.7
D-ribulose
pH 7.0, 25°C
6.3
D-ribulose
pH 7.0, 25°C
6.3
D-ribulose
pH 7.0, 25°C
7.8
D-ribulose
pH 7.0, 25°C
105
D-ribulose
pH 7.0, 30°C, recombinant enzyme
14
D-threitol
pH 7.0, 25°C
16
D-threitol
pH 7.0, 25°C
18
D-threitol
pH 7.0, 25°C
34
D-threitol
pH 7.0, 25°C
37
D-threitol
pH 7.0, 25°C
0.68
D-threose
pH 7.0, temperature not specified in the publication
1.9
D-threose
pH 7.0, 25°C
2.4
D-threose
pH 7.0, 25°C
2.7
D-threose
pH 7.0, 25°C
2.58
D-xylulose
pH 7.0, temperature not specified in the publication
4.8
D-xylulose
pH 7.0, 25°C
12
D-xylulose
pH 7.0, 25°C
12
D-xylulose
pH 7.0, 25°C
18
D-xylulose
pH 7.0, 25°C
18
D-xylulose
pH 7.0, 25°C
0.077
diacetyl
pH 7.0, 25°C, wild-type enzyme
0.077
diacetyl
pH 7.0, 25°C
0.0945
diacetyl
wild type enzyme, in 10 mM potassium phosphate buffer
0.2
diacetyl
pH 7.0, 25°C
0.22
diacetyl
mutant enzyme C138A, in 10 mM potassium phosphate buffer
0.52
diacetyl
pH 7.0, 25°C
0.67
diacetyl
pH 7.0, 25°C
0.78
diacetyl
-
pH 7.0, 25°C, wild-type enzyme
1.1
diacetyl
pH 7.0, 25°C
1.2
diacetyl
-
pH 7.0, 25°C, mutant H146L
2.6
diacetyl
-
pH 7.0, 25°C, mutant N190V
2.7
diacetyl
-
pH 7.0, 25°C, mutant N190V/W191S/Q137M/L143F/H146L
3
diacetyl
-
pH 7.0, 25°C, mutant Q137M
5.2
diacetyl
-
pH 7.0, 25°C, mutant W191F
6.2
diacetyl
-
pH 7.0, 25°C, mutant L143F
9.6
diacetyl
-
pH 7.0, 25°C, mutant Q137M/L143F/H146L
11
diacetyl
-
pH 7.0, 25°C, mutant Q137M/L143F
16
diacetyl
-
pH 7.0, 25°C, mutant N190V/W191S
26
diacetyl
pH 7.0, 25°C, mutant N107D
31
diacetyl
pH 7.0, 25°C, mutant N107L
42
diacetyl
-
pH 7.0, 25°C, mutant W191S
1.6
dihydroxyacetone
pH 7.0, 25°C
36
dihydroxyacetone
pH 7.0, 25°C
47
dihydroxyacetone
pH 7.0, 25°C
60
dihydroxyacetone
pH 7.0, 25°C
60
dihydroxyacetone
pH 7.0, 25°C
1.2
DL-glyceraldehyde
pH 7.0, 25°C
1.4
DL-glyceraldehyde
pH 7.0, 25°C
2.7
DL-glyceraldehyde
pH 7.0, 25°C
5.1
DL-glyceraldehyde
pH 7.0, 25°C
6
DL-glyceraldehyde
pH 7.0, 25°C
0.17
L-erythrulose
pH 7.0, temperature not specified in the publication
2
L-erythrulose
pH 7.0, 25°C
2.5
L-erythrulose
pH 7.0, 25°C
2.9
L-erythrulose
pH 7.0, 25°C
4.8
L-erythrulose
pH 7.0, 25°C
5.5
L-erythrulose
pH 7.0, 25°C
2.9
L-threose
pH 7.0, 25°C
4.2
L-threose
pH 7.0, 25°C
4.3
L-threose
pH 7.0, 25°C
5.6
L-threose
pH 7.0, 25°C
8.3
L-threose
pH 7.0, 25°C
0.0099
L-xylitol
-
pH 7.0, 25°C, mutant Y149F
0.011
L-xylitol
-
pH 7.0, 25°C, wild-type enzyme
0.013
L-xylitol
-
pH 7.0, 25°C, mutant S136A
0.085
L-xylitol
-
pH 7.0, 25°C, mutant K153M
7.2
L-xylitol
pH 9.0, 30°C, purified recombinant enzyme
0.05
L-xylulose
pH 7.0, 25°C
0.092
L-xylulose
-
pH 7.0, 25°C, mutant H146L
0.14
L-xylulose
-
pH 7.0, 25°C, wild-type enzyme and mutant L143F
0.21
L-xylulose
pH 7.0, 25°C
0.23
L-xylulose
pH 7.0, 25°C
0.24
L-xylulose
pH 7.0, 25°C
0.26
L-xylulose
pH 7.0, 25°C
0.31
L-xylulose
-
pH 7.0, 25°C, mutant N190V
0.33
L-xylulose
-
pH 7.0, 25°C, mutant Q137M
0.66
L-xylulose
pH 7.0, temperature not specified in the publication
3.6
L-xylulose
-
pH 7.0, 25°C, mutant Q137M/L143F
7.2
L-xylulose
-
pH 7.0, 25°C, mutant W191F
8.71
L-xylulose
pH 7.0, 25°C, native enzyme
9.6
L-xylulose
pH 7.0, 30°C, purified recombinant enzyme
13.2
L-xylulose
pH 7.0, 25°C, recombinant enzyme
16
L-xylulose
pH 7.0, 30°C, recombinant enzyme
25
L-xylulose
-
pH 7.0, 22°C
0.85
NAD+
pH 7.0, 25°C
0.12
NADH
pH 7.0, 25°C
0.00067
NADP+
-
pH 7.0, 25°C, mutant S136A
0.0013
NADP+
-
pH 7.0, 25°C, mutant Y149F
0.003
NADP+
-
pH 7.0, 25°C, wild-type enzyme
0.117
NADP+
-
pH 7.0, 25°C, mutant K153M
0.002
NADPH
pH 7.0, 25°C, wild-type enzyme
0.002
NADPH
-
pH 7.0, 25°C, mutant Y149F
0.0046
NADPH
-
pH 7.0, 25°C, mutant S136A
0.007
NADPH
-
pH 7.0, 25°C, wild-type enzyme
0.053
NADPH
-
pH 7.0, 25°C, mutant K153M
0.13
NADPH
pH 7.0, 30°C, recombinant enzyme, with L-xylulose
95
NADPH
pH 7.0, 25°C, mutant N107D
97
NADPH
pH 7.0, 25°C, mutant N107L
10
xylitol
pH 7.0, 25°C
100
xylitol
pH 7.0, 30°C, recombinant enzyme
225
xylitol
pH 9.6, 25°C, recombinant enzyme
253
xylitol
pH 9.6, 25°C, native enzyme
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N107D
site-directed mutagenesis, active site residue mutant, inactive
N107L
site-directed mutagenesis, active site residue mutant, inactive
D238E
-
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
D238E/L242W
-
site-directed mutagenesis, mutation leads to complete prevention of cold inactivation, mutant exists in tetrameric form at low temperature
D238E/L242W/T244C
-
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
L242W
-
site-directed mutagenesis, mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
L242W/T244C
-
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
T244C
-
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
K153M
-
site-directed mutagenesis, active site mutant, complete loss of activity
N190V
-
site-directed mutagenesis, altered activity
N190V/W191S
-
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity
N190V/W191S/Q137M/L143F/H146L
-
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows high 3-ketosteroid reductase activity
Q137M
-
site-directed mutagenesis, altered activity, stable against cold inactivation
Q137M/F241L
-
site-directed mutagenesis, altered activity, sensitive to cold inactivation like the wild-type enzyme
Q137M/L143F
-
site-directed mutagenesis, increased Km for L-xylulose compared to the wild-type
Q137M/L143F/H146L
-
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows 3-ketosteroid reductase activity
S136A
-
site-directed mutagenesis, active site mutant, complete loss of activity
Y149F
-
site-directed mutagenesis, active site mutant, complete loss of activity
D207/I208R/F209S
-
kcat/Km of mutant enzyme for NAD+ dropps 15fold compared with the native enzyme, kcat/Km for NADP+ increases up to 4100fold
S96C/S99C/Y102C/D207A/I208R/F209S
-
mutation produces a further 4fold improvement in the kcat/Km for NADP+ compared to mutant enzyme D207/I208R/F209S
H146L
-
site-directed mutagenesis, altered activity
H146L
-
IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 7.8fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 6.7fold higher than wild-type value
L143F
-
site-directed mutagenesis, altered activity
L143F
-
IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 8.3fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 1.9fold higher than wild-type value
W191F
-
site-directed mutagenesis, altered activity
W191F
-
IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 3.4fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 7.3fold higher than wild-type value
W191S
-
site-directed mutagenesis, altered activity
W191S
-
IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 13fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 1.5fold lower than wild-type value
additional information
library screening and isolation of a dhs-21 deletion mutant
additional information
-
library screening and isolation of a dhs-21 deletion mutant
additional information
xylitol is produced from xylose via the NADPH dependent reductase, a two-stage dynamic control over feedback regulatory mechanisms improves NADPH flux and xylitol biosynthesis in engineered Escherichia coli, method evaluation, overview. Comparison of two approaches to optimize xylitol biosynthesis: a stoichiometric approach wherein competitive fluxes are decreased, and a regulatory approach wherein the levels of key regulatory metabolites are reduced. The stoichiometric and regulatory approaches lead to a 20fold and 90fold improvement in xylitol production, respectively. Strains with reduced levels of enoyl-ACP reductase and glucose-6-phosphate dehydrogenase, lead to altered metabolite pools resulting in the activation of the membrane bound transhydrogenase and an NADPH generation pathway, consisting of pyruvate ferredoxin oxidoreductase coupled with NADPH dependent ferredoxin reductase, causing increased NADPH fluxes, despite a reduction in NADPH pools. These strains produce titers of 200 g/l of xylitol from xylose at 86% of theoretical yield in instrumented bioreactors
additional information
-
engineering of strain YZJ088 for ethanol production via the NADP(H)-preferring xylose reductase-xylitol dehydrogenase pathway in the thermotolerant yeast Kluyveromyces marxianus, method overview
additional information
-
engineering of strain YZJ088 for ethanol production via the NADP(H)-preferring xylose reductase-xylitol dehydrogenase pathway in the thermotolerant yeast Kluyveromyces marxianus, method overview
-
additional information
Escherichia coli strain WZ04 is first constructed by a simultaneous deletion-insertion strategy involving CRISPR/Cas9 markerless gene-editing technology, replacing ptsG, xylAB and ptsF in wild-type Escherichia coli strain W3110 with three mutated xylose reductase genes (xr) from Neurospora crassa. In a second approach, the pfkA, pfkB, pgi and/or sthA genes are deleted and replaced by xr to investigate the influence of carbon flux toward the pentose phosphate pathway and/or transhydrogenase activity on NADPH generation. The deletion of pfkA/pfkB significantly improves NADPH supply, but minimally influences cell growth. The effects of insertion position and copy number of xr are examined by a quantitative real-time PCR and a shake-flask fermentation experiment. In a fed-batch fermentation experiment with a 15-l bioreactor, strain WZ51 produces 131.6 g/l xylitol from hemicellulosic hydrolysate (xylitol productivity: 2.09 g/l/h). The biotransformation process involves resting cell catalysis with pure xylose as the substrate, but not hemicellulosic hydrolysate. Cofactor ratios are measured for single gene replacement strains and strains with combinatorial gene replacements, all based on strain WZ04, overview
additional information
-
Escherichia coli strain WZ04 is first constructed by a simultaneous deletion-insertion strategy involving CRISPR/Cas9 markerless gene-editing technology, replacing ptsG, xylAB and ptsF in wild-type Escherichia coli strain W3110 with three mutated xylose reductase genes (xr) from Neurospora crassa. In a second approach, the pfkA, pfkB, pgi and/or sthA genes are deleted and replaced by xr to investigate the influence of carbon flux toward the pentose phosphate pathway and/or transhydrogenase activity on NADPH generation. The deletion of pfkA/pfkB significantly improves NADPH supply, but minimally influences cell growth. The effects of insertion position and copy number of xr are examined by a quantitative real-time PCR and a shake-flask fermentation experiment. In a fed-batch fermentation experiment with a 15-l bioreactor, strain WZ51 produces 131.6 g/l xylitol from hemicellulosic hydrolysate (xylitol productivity: 2.09 g/l/h). The biotransformation process involves resting cell catalysis with pure xylose as the substrate, but not hemicellulosic hydrolysate. Cofactor ratios are measured for single gene replacement strains and strains with combinatorial gene replacements, all based on strain WZ04, overview
additional information
-
Escherichia coli strain WZ04 is first constructed by a simultaneous deletion-insertion strategy involving CRISPR/Cas9 markerless gene-editing technology, replacing ptsG, xylAB and ptsF in wild-type Escherichia coli strain W3110 with three mutated xylose reductase genes (xr) from Neurospora crassa. In a second approach, the pfkA, pfkB, pgi and/or sthA genes are deleted and replaced by xr to investigate the influence of carbon flux toward the pentose phosphate pathway and/or transhydrogenase activity on NADPH generation. The deletion of pfkA/pfkB significantly improves NADPH supply, but minimally influences cell growth. The effects of insertion position and copy number of xr are examined by a quantitative real-time PCR and a shake-flask fermentation experiment. In a fed-batch fermentation experiment with a 15-l bioreactor, strain WZ51 produces 131.6 g/l xylitol from hemicellulosic hydrolysate (xylitol productivity: 2.09 g/l/h). The biotransformation process involves resting cell catalysis with pure xylose as the substrate, but not hemicellulosic hydrolysate. Cofactor ratios are measured for single gene replacement strains and strains with combinatorial gene replacements, all based on strain WZ04, overview
-
additional information
-
Escherichia coli strain WZ04 is first constructed by a simultaneous deletion-insertion strategy involving CRISPR/Cas9 markerless gene-editing technology, replacing ptsG, xylAB and ptsF in wild-type Escherichia coli strain W3110 with three mutated xylose reductase genes (xr) from Neurospora crassa. In a second approach, the pfkA, pfkB, pgi and/or sthA genes are deleted and replaced by xr to investigate the influence of carbon flux toward the pentose phosphate pathway and/or transhydrogenase activity on NADPH generation. The deletion of pfkA/pfkB significantly improves NADPH supply, but minimally influences cell growth. The effects of insertion position and copy number of xr are examined by a quantitative real-time PCR and a shake-flask fermentation experiment. In a fed-batch fermentation experiment with a 15-l bioreactor, strain WZ51 produces 131.6 g/l xylitol from hemicellulosic hydrolysate (xylitol productivity: 2.09 g/l/h). The biotransformation process involves resting cell catalysis with pure xylose as the substrate, but not hemicellulosic hydrolysate. Cofactor ratios are measured for single gene replacement strains and strains with combinatorial gene replacements, all based on strain WZ04, overview
-
additional information
-
Escherichia coli strain WZ04 is first constructed by a simultaneous deletion-insertion strategy involving CRISPR/Cas9 markerless gene-editing technology, replacing ptsG, xylAB and ptsF in wild-type Escherichia coli strain W3110 with three mutated xylose reductase genes (xr) from Neurospora crassa. In a second approach, the pfkA, pfkB, pgi and/or sthA genes are deleted and replaced by xr to investigate the influence of carbon flux toward the pentose phosphate pathway and/or transhydrogenase activity on NADPH generation. The deletion of pfkA/pfkB significantly improves NADPH supply, but minimally influences cell growth. The effects of insertion position and copy number of xr are examined by a quantitative real-time PCR and a shake-flask fermentation experiment. In a fed-batch fermentation experiment with a 15-l bioreactor, strain WZ51 produces 131.6 g/l xylitol from hemicellulosic hydrolysate (xylitol productivity: 2.09 g/l/h). The biotransformation process involves resting cell catalysis with pure xylose as the substrate, but not hemicellulosic hydrolysate. Cofactor ratios are measured for single gene replacement strains and strains with combinatorial gene replacements, all based on strain WZ04, overview
-
additional information
-
Escherichia coli strain WZ04 is first constructed by a simultaneous deletion-insertion strategy involving CRISPR/Cas9 markerless gene-editing technology, replacing ptsG, xylAB and ptsF in wild-type Escherichia coli strain W3110 with three mutated xylose reductase genes (xr) from Neurospora crassa. In a second approach, the pfkA, pfkB, pgi and/or sthA genes are deleted and replaced by xr to investigate the influence of carbon flux toward the pentose phosphate pathway and/or transhydrogenase activity on NADPH generation. The deletion of pfkA/pfkB significantly improves NADPH supply, but minimally influences cell growth. The effects of insertion position and copy number of xr are examined by a quantitative real-time PCR and a shake-flask fermentation experiment. In a fed-batch fermentation experiment with a 15-l bioreactor, strain WZ51 produces 131.6 g/l xylitol from hemicellulosic hydrolysate (xylitol productivity: 2.09 g/l/h). The biotransformation process involves resting cell catalysis with pure xylose as the substrate, but not hemicellulosic hydrolysate. Cofactor ratios are measured for single gene replacement strains and strains with combinatorial gene replacements, all based on strain WZ04, overview
-
additional information
-
Escherichia coli strain WZ04 is first constructed by a simultaneous deletion-insertion strategy involving CRISPR/Cas9 markerless gene-editing technology, replacing ptsG, xylAB and ptsF in wild-type Escherichia coli strain W3110 with three mutated xylose reductase genes (xr) from Neurospora crassa. In a second approach, the pfkA, pfkB, pgi and/or sthA genes are deleted and replaced by xr to investigate the influence of carbon flux toward the pentose phosphate pathway and/or transhydrogenase activity on NADPH generation. The deletion of pfkA/pfkB significantly improves NADPH supply, but minimally influences cell growth. The effects of insertion position and copy number of xr are examined by a quantitative real-time PCR and a shake-flask fermentation experiment. In a fed-batch fermentation experiment with a 15-l bioreactor, strain WZ51 produces 131.6 g/l xylitol from hemicellulosic hydrolysate (xylitol productivity: 2.09 g/l/h). The biotransformation process involves resting cell catalysis with pure xylose as the substrate, but not hemicellulosic hydrolysate. Cofactor ratios are measured for single gene replacement strains and strains with combinatorial gene replacements, all based on strain WZ04, overview
-
additional information
-
several mutants per site-directed mutagenesis to change the coenzyme binding specificity, mutants showed reduced NAD+ specificity
additional information
-
enzyme XDH is changed from NAD+-dependent to NADP+-dependent, xylitol accumulation is reduced and ethanol production improved using protein engineering for reversing the dependency of XDH from NAD+ to NADP+. Construction of a set of recombinant Saccharomyces cerevisiae carrying a mutated strictly NADPH-dependent XR and NADP+-dependent XDH genes with overexpression of endogenous xylulokinase (XK), effects of complete NADPH/NADP+ recycling on ethanol fermentation and xylitol accumulation, overview. The mutated strains demonstrate 0% and 10% improvement in ethanol production, and reduced xylitol accumulation, ranging 34.4-54.7% compared with the control strain
additional information
deletion of gene lxr3 leads to a significant reduction in NADPH specific LXR activity after replacement to both media containing L-arabinose
additional information
-
deletion of gene lxr3 leads to a significant reduction in NADPH specific LXR activity after replacement to both media containing L-arabinose
additional information
-
deletion of gene lxr3 leads to a significant reduction in NADPH specific LXR activity after replacement to both media containing L-arabinose
-
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Hickman, J.; Ashwell, G.
A sensitive and stereospecific enzymatic assay for xylulose
J. Biol. Chem.
234
758-761
1959
Cavia porcellus
brenda
Alizade, M.A.; Brendel, K.; Gaede, K.
Chirality of xylitol-oxidizing enzymes from mammalian liver
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67
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1976
Cavia porcellus
brenda
Doten, R.C.; Mortlock, R.P.
Inducible xylitol dehydrogenases in enteric bacteria
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845-848
1985
Erwinia sp., Erwinia sp. 4D2P
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Characterization of xylitol-utilizing mutants of Erwinia uredovora
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529-533
1985
Pantoea ananatis
brenda
Lowe, C.R.; Mosbach, K.; Dean, P.D.G.
Some applications of insolubilised cofactors to the purification of pyridine nucleotide-dependent dehydrogenases
Biochem. Biophys. Res. Commun.
48
1004-1010
1972
Saccharomyces cerevisiae
brenda
Hollmann, S.; Touster, O.
The L-xylulose-xylitol enzyme and other polyol dehydrogenases of guinea pig liver mitochondria
J. Biol. Chem.
225
87-102
1957
Cavia porcellus
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Touster, O.; Reynolds, V.H.; Hutcheson, R.M.
The reduction of L-xylulose to xylitol by guinea pig liver mitochondria
J. Biol. Chem.
221
697-709
1954
Cavia porcellus
brenda
Witteveen, C.F.B.; Weber, F.; Busink, R.; Visser, J.
Isolation and characterization of two xylitol dehydrogenases from Aspergillus niger
Microbiology
140
1679-1685
1994
Aspergillus niger
-
brenda
Metzger, M.H.; Hollenberg, C.P.
Amino acid substitutions in the yeast Pichia stipitis xylitol dehydrogenase coenzyme-binding domain affect the coenzyme specificity
Eur. J. Biochem.
228
50-54
1995
Scheffersomyces stipitis
brenda
Ishikura, S.; Isaji, T.; Usami, N.; Kitahara, K.; Nakagawa, J.; Hara, A.
Molecular cloning, expression and tissue distribution of hamster diacetyl reductase. Identity with L-xylulose reductase
Chem. Biol. Interact.
130-132
879-889
2001
Cricetinae
brenda
Ishikura, S.; Usami, N.; El-Kabbani, O.; Hara, A.
Structural determinant for cold inactivation of rodent L-xylulose reductase
Biochem. Biophys. Res. Commun.
308
68-72
2003
Homo sapiens, Mus musculus
brenda
Carbone, V.; Darmanin, C.; Ishikura, S.; Hara, A.; El-Kabbani, O.
Structure-based design of inhibitors of human L-xylulose reductase modelled into the active site of the enzyme
Bioorg. Med. Chem. Lett.
13
1469-1474
2003
Homo sapiens
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Ishikura, S.; Isaji, T.; Usami, N.; Nakagawa, J.; El-Kabbani, O.; Hara, A.
Identification of amino acid residues involved in substrate recognition of L-xylulose reductase by site-directed mutagenesis
Chem. Biol. Interact.
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2003
Rattus norvegicus
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Nakagawa, J.; Ishikura, S.; Asami, J.; Isaji, T.; Usami, N.; Hara, A.; Sakurai, T.; Tsuritani, K.; Oda, K.; Takahashi, M.; Yoshimoto, M.; Otsuka, N.; Kitamura, K.
Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney
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Cavia porcellus (Q920N9), Cavia porcellus, Homo sapiens (Q7Z4W1), Homo sapiens, Mesocricetus auratus (Q91XV4), Mus musculus (Q91X52), Mus musculus, Rattus norvegicus (Q920P0)
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Verho, R.; Putkonen, M.; Londesborough, J.; Penttil, M.; Richard, P.
A novel NADH-linked L-xylulose reductase in the L-arabinose catabolic pathway of yeast
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Ambrosiozyma monospora (Q70FD1), Ambrosiozyma monospora
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Saint-Cyr, A.; Legare, C.; Frenette, G.; Gaudreault, C.; Sullivan, R.
P26h and dicarbonyl/L-xylulose reductase are two distinct proteins present in the hamster epididymis
Mol. Reprod. Dev.
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Mesocricetus auratus
brenda
El-Kabbani, O.; Ishikura, S.; Darmanin, C.; Carbone, V.; Chung, R.P.T.; Usami, N.; Hara, A.
Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis
Proteins
55
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2004
Homo sapiens (Q7Z4W1), Homo sapiens
brenda
Matsunaga, T.; Shintani, S.; Hara, A.
Multiplicity of mammalian reductases for xenobiotic carbonyl compounds
Drug Metab. Pharmacokinet.
21
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Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Sudo, T.; Ishii, A.; Asami, J.; Uematsu, Y.; Saitoh, M.; Nakamura, A.; Tada, N.; Ohnuki, T.; Komurasaki, T.; Nakagawa, J.
Transgenic mice over-expressing dicarbonyl/L-xylulose reductase gene crossed with KK-A(y) diabetic model mice: an animal model for the metabolism of renal carbonyl compounds
Exp. Anim.
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Mus musculus
brenda
El-Kabbani, O.; Carbone, V.; Darmanin, C.; Ishikura, S.; Hara, A.
Structure of the tetrameric form of human L-xylulose reductase: probing the inhibitor-binding site with molecular modeling and site-directed mutagenesis
Proteins
60
424-432
2005
Homo sapiens, Rattus norvegicus
brenda
Nair, N.; Zhao, H.
Biochemical characterization of an L-Xylulose reductase from Neurospora crassa
Appl. Environ. Microbiol.
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Neurospora crassa
brenda
Matsunaga, T.; Kamiya, T.; Sumi, D.; Kumagai, Y.; Kalyanaraman, B.; Hara, A.
L-Xylulose reductase is involved in 9,10-phenanthrenequinone-induced apoptosis in human T lymphoma cells
Free Radic. Biol. Med.
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Homo sapiens
brenda
Matsushika, A.; Watanabe, S.; Kodaki, T.; Makino, K.; Sawayama, S.
Bioethanol production from xylose by recombinant Saccharomyces cerevisiae expressing xylose reductase, NADP(+)-dependent xylitol dehydrogenase, and xylulokinase
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2008
Scheffersomyces stipitis
brenda
Hou, J.; Shen, Y.; Li, X.P.; Bao, X.M.
Effect of the reversal of coenzyme specificity by expression of mutated Pichia stipitis xylitol dehydrogenase in recombinant Saccharomyces cerevisiae
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Scheffersomyces stipitis
brenda
Matsushika, A.; Inoue, H.; Watanabe, S.; Kodaki, T.; Makino, K.; Sawayama, S.
Efficient bioethanol production by a recombinant flocculent Saccharomyces cerevisiae strain with a genome-integrated NADP+-dependent xylitol dehydrogenase gene
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Scheffersomyces stipitis
brenda
Matsushika, A.; Watanabe, S.; Kodaki, T.; Makino, K.; Inoue, H.; Murakami, K.; Takimura, O.; Sawayama, S.
Expression of protein engineered NADP+-dependent xylitol dehydrogenase increases ethanol production from xylose in recombinant Saccharomyces cerevisiae
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Scheffersomyces stipitis
brenda
Hou, J.; Vemuri, G.N.; Bao, X.; Olsson, L.
Impact of overexpressing NADH kinase on glucose and xylose metabolism in recombinant xylose-utilizing Saccharomyces cerevisiae
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2009
Scheffersomyces stipitis
brenda
Krahulec, S.; Klimacek, M.; Nidetzky, B.
Engineering of a matched pair of xylose reductase and xylitol dehydrogenase for xylose fermentation by Saccharomyces cerevisiae
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Yamadazyma tenuis
brenda
Zhao, H.T.; Endo, S.; Ishikura, S.; Chung, R.; Hogg, P.J.; Hara, A.; El-Kabbani, O.
Structure/function analysis of a critical disulfide bond in the active site of L-xylulose reductase
Cell. Mol. Life Sci.
66
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Homo sapiens (Q7Z4W1)
brenda
Branco, R.; dos Santos, J.; Sarrouh, B.; Rivaldi, J.; Pessoa Jr., A.; da Silva, S.
Profiles of xylose reductase, xylitol dehydrogenase and xylitol production under different oxygen transfer volumetric coefficient values
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Meyerozyma guilliermondii, Meyerozyma guilliermondii FTI
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brenda
Gurpilhares, D.B.; Hasmann, F.A.; Pessoa, A.; Roberto, I.C.
The behavior of key enzymes of xylose metabolism on the xylitol production by Candida guilliermondii grown in hemicellulosic hydrolysate
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Meyerozyma guilliermondii
brenda
Mojzita, D.; Vuoristo, K.; Koivistoinen, O.M.; Penttilae, M.; Richard, P.
The true L-xylulose reductase of filamentous fungi identified in Aspergillus niger
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Aspergillus niger
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Metz, B.; Mojzita, D.; Herold, S.; Kubicek, C.P.; Richard, P.; Seiboth, B.
A novel L-xylulose reductase essential for L-arabinose catabolism in Trichoderma reesei
Biochemistry
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2013
Trichoderma reesei (Q8NK50), Trichoderma reesei, Trichoderma reesei QM9414 (Q8NK50)
brenda
Son, l.e..T.; Ko, K.M.; Cho, J.H.; Singaravelu, G.; Chatterjee, I.; Choi, T.W.; Song, H.O.; Yu, J.R.; Park, B.J.; Lee, S.K.; Ahnn, J.
DHS-21, a dicarbonyl/L-xylulose reductase (DCXR) ortholog, regulates longevity and reproduction in Caenorhabditis elegans
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Caenorhabditis elegans (Q21929), Caenorhabditis elegans
brenda
Zheng, Y.; Yu, X.; Li, T.; Xiong, X.; Chen, S.
Induction of D-xylose uptake and expression of NAD(P)H-linked xylose reductase and NADP+-linked xylitol dehydrogenase in the oleaginous microalga Chlorella sorokiniana
Biotechnol. Biofuels
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Chlorella sorokiniana, Chlorella sorokiniana UTEX 1602
brenda
Zhang, B.; Zhang, J.; Wang, D.; Gao, X.; Sun, L.; Hong, J.
Data for rapid ethanol production at elevated temperatures by engineered thermotolerant Kluyveromyces marxianus via the NADP(H)-preferring xylose reductase-xylitol dehydrogenase pathway
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Kluyveromyces marxianus, Kluyveromyces marxianus YZJ088
brenda
Khattab, S.M.; Saimura, M.; Kodaki, T.
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Scheffersomyces stipitis
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Yamasaki-Yashiki, S.; Komeda, H.; Hoshino, K.; Asano, Y.
Characterization and gene cloning of L-xylulose reductase involved in L-arabinose catabolism from the pentose-fermenting fungus Rhizomucor pusillus
Biosci. Biotechnol. Biochem.
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Rhizomucor pusillus (A0A0M4UR95), Rhizomucor pusillus, Rhizomucor pusillus NBRC 4578 (A0A0M4UR95), Rhizomucor pusillus NBRC 4578
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Yuan, X.; Wang, J.; Lin, J.; Yang, L.; Wu, M.
Efficient production of xylitol by the integration of multiple copies of xylose reductase gene and the deletion of Embden-Meyerhof-Parnas pathway-associated genes to enhance NADPH regeneration in Escherichia coli
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Neurospora crassa (Q7SD67), Neurospora crassa, Neurospora crassa CBS 708.71 (Q7SD67), Neurospora crassa 74-OR23-1A (Q7SD67), Neurospora crassa DSM 1257 (Q7SD67), Neurospora crassa ATCC 24698 (Q7SD67), Neurospora crassa FGSC 987 (Q7SD67)
brenda
Li, S.; Ye, Z.; Moreb, E.A.; Hennigan, J.N.; Castellanos, D.B.; Yang, T.; Lynch, M.D.
Dynamic control over feedback regulatory mechanisms improves NADPH flux and xylitol biosynthesis in engineered E. coli
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2021
Escherichia coli (A0A0E3ZP28)
brenda