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2-deoxy-D-galactose + NADH
?
-
-
-
?
2-deoxy-D-galactose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
2-deoxy-D-glucose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
2-deoxy-D-ribose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
5,6-dideoxy-5,6-difluoro-D-glucofuranose + NADPH + H+
? + NADP+
5,6-dideoxy-5-fluoro-D-glucofuranose + NADPH + H+
? + NADP+
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose + NADPH + H+
? + NADP+
5,6-dideoxy-D-xylo-hexofuranose + NADPH + H+
? + NADP+
5-azido-5-deoxy-D-xylofuranose + NADPH + H+
? + NADP+
5-deoxy-D-xylofuranose + NADPH + H+
? + NADP+
5-fluoro-5-deoxy-D-xylofuranose + NADPH + H+
? + NADP+
5-hydroxymethylfurfural + NADH + H+
(furan-2,5-diyl)dimethanol + NAD+
low activity
-
-
r
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose + NADPH + H+
? + NADP+
6-azido-5,6-dideoxy-D-xylo-hexofuranose + NADPH + H+
? + NADP+
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
r
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
best substrate
-
-
r
butanal + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
cyclohexanecarboxaldehyde + NADPH + H+
? + NADP+
D-erythrose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-erythrose + NADPH + H+
erythritol + NADP+
-
-
-
r
D-fructose + NADPH + H+
sorbitol + NADP+
D-fucose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-galactose + NADH
?
-
-
-
?
D-galactose + NADH + H+
?
48% of the activity compared to D-xylose (with NADH as cofactor)
-
-
?
D-galactose + NADH + H+
? + NAD+
D-galactose + NADPH + H+
?
D-galactose + NADPH + H+
? + NADP+
D-galactose + NADPH + H+
galactitol + NADP+
D-glucose + NADH
?
-
-
-
?
D-glucose + NADH + H+
?
10 of the activity compared to D-xylose (with NADH as cofactor)
-
-
?
D-glucose + NADPH + H+
? + NADP+
D-glucose + NADPH + H+
glucitol + NADP+
D-glyceraldehyde + NADH
?
-
-
-
?
D-lyxose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-mannose + NADH + H+
?
8% of the activity compared to D-xylose (with NADH as cofactor)
-
-
?
D-ribose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-ribose + NADPH + H+
? + NADP+
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
D-xylose + NADH + H+
xylitol + NAD+
D-xylose + NADPH + H+
xylitol + NADP+
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
furfural + NADH + H+
(furan-2-yl)methanol + NAD+
-
-
-
r
L-arabinose + NADPH + H+
arabitol + NADP+
L-arabinose + NADPH + H+
L-arabinitol + NADP+
L-arabinose + NADPH + H+
L-arabitol + NADP+
-
-
-
-
?
L-lyxose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
L-threose + NADPH + H+
threitol + NADP+
-
-
-
r
oenanthaldehyde + NADPH + H+
? + NADP+
pentanal + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
propionaldehyde + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
xylitol + NAD+
D-xylose + NADH + H+
xylitol + NADP+
D-xylose + NADPH + H+
xylulose + NADH + H+
? + NAD+
-
-
-
r
additional information
?
-
5,6-dideoxy-5,6-difluoro-D-glucofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5,6-dideoxy-5,6-difluoro-D-glucofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5,6-dideoxy-5-fluoro-D-glucofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5,6-dideoxy-5-fluoro-D-glucofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5,6-dideoxy-D-xylo-hexofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5,6-dideoxy-D-xylo-hexofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5-azido-5-deoxy-D-xylofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5-azido-5-deoxy-D-xylofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5-deoxy-D-xylofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5-deoxy-D-xylofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5-fluoro-5-deoxy-D-xylofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5-fluoro-5-deoxy-D-xylofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
6-azido-5,6-dideoxy-D-xylo-hexofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
6-azido-5,6-dideoxy-D-xylo-hexofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
cyclohexanecarboxaldehyde + NADPH + H+
? + NADP+
-
-
-
-
?
cyclohexanecarboxaldehyde + NADPH + H+
? + NADP+
-
-
-
-
?
D-fructose + NADPH + H+
sorbitol + NADP+
-
-
-
r
D-fructose + NADPH + H+
sorbitol + NADP+
-
-
-
r
D-galactose + NADH + H+
? + NAD+
53% of the activity with D-xylose
-
-
?
D-galactose + NADH + H+
? + NAD+
53% of the activity with D-xylose
-
-
?
D-galactose + NADPH + H+
?
-
D-xylose reductase 1: 49% of the activity with D-xylose, D-xylose reductase 2: 40% of the activity with D-xylose, D-xylose reductase 3: 33% of the activity with D-xylose
-
-
?
D-galactose + NADPH + H+
?
-
D-xylose reductase 1: 49% of the activity with D-xylose, D-xylose reductase 2: 40% of the activity with D-xylose, D-xylose reductase 3: 33% of the activity with D-xylose
-
-
?
D-galactose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-galactose + NADPH + H+
? + NADP+
-
-
-
-
?
D-galactose + NADPH + H+
? + NADP+
-
-
-
-
?
D-galactose + NADPH + H+
galactitol + NADP+
-
-
-
-
r
D-galactose + NADPH + H+
galactitol + NADP+
-
-
-
r
D-galactose + NADPH + H+
galactitol + NADP+
-
-
-
r
D-glucose + NADPH + H+
?
-
D-xylose reductase 1: 10% of the activity with D-xylose, D-xylose reductase 2: 11% of the activity with D-xylose, D-xylose reductase 3: 11% of the activity with D-xylose
-
-
?
D-glucose + NADPH + H+
?
-
D-xylose reductase 1: 10% of the activity with D-xylose, D-xylose reductase 2: 11% of the activity with D-xylose, D-xylose reductase 3: 11% of the activity with D-xylose
-
-
?
D-glucose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-glucose + NADPH + H+
? + NADP+
38% of the activity with D-xylose
-
-
?
D-glucose + NADPH + H+
? + NADP+
38% of the activity with D-xylose
-
-
?
D-glucose + NADPH + H+
glucitol + NADP+
-
-
-
r
D-glucose + NADPH + H+
glucitol + NADP+
-
-
-
r
D-ribose + NADPH + H+
? + NADP+
84% of the activity with D-xylose
-
-
?
D-ribose + NADPH + H+
? + NADP+
84% of the activity with D-xylose
-
-
?
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
-
-
-
-
?
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
-
xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by a NAD+-linked xylulose dehydrogenase, EC 1.1.1.9
-
-
?
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
-
-
-
-
?
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
-
xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by a NAD+-linked xylulose dehydrogenase, EC 1.1.1.9
-
-
?
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
-
-
-
-
?
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
-
xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by a NAD+-linked xylulose dehydrogenase, EC 1.1.1.9
-
-
?
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
-
-
-
-
?
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
-
?
D-xylose + NADH + H+
xylitol + NAD+
NADPH is the preferred cofactor
-
-
?
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
kcat of wilde-type enzyme increases by a factor of 1.73 when NADPH replaces NADH
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
using a modified iterative protein redesign and optimization workflow, a sets of mutations is identified that change the nicotinamide cofactor specificity of xylose reductase (CbXR) from its physiological preference for NADPH, to the alternate cofactor NADH
-
-
?
D-xylose + NADH + H+
xylitol + NAD+
-
reaction is catalyzed by dual specific xylose reductase (dsXR), reaction is not catalyzed by NADPH-dependent monospecific xylose reductase (msXR)
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
kinetic mechanism of xylose reductase is iso-ordered bi bi
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
NADPH is the preferred cofactor, specific for D-xylose
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
D-xylose binding mode of SsXR is elucidated by molecular docking simulations of SsXR with the D-xylose substrate revealing that D-xylose fits well into the predicted substrate binding pocket. The D-xylose binding pocket consists of 10 residues: Trp20, Asp47, Trp79, His110, Phe111, Phe128, Phe221, Leu224, Asn306, and Trp311. The Asp47 residue contributes to the stabilization of two hydroxyl groups (OH2 and OH3), and the aldehyde group of D-xylose is stabilized by Asn306 through hydrogen bonding. The residues involved in formation of the D-xylose binding pocket are confirmed by site-directed mutagenesis experiments
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
D-xylose binding mode of SsXR is elucidated by molecular docking simulations of SsXR with the D-xylose substrate revealing that D-xylose fits well into the predicted substrate binding pocket. The D-xylose binding pocket consists of 10 residues: Trp20, Asp47, Trp79, His110, Phe111, Phe128, Phe221, Leu224, Asn306, and Trp311. The Asp47 residue contributes to the stabilization of two hydroxyl groups (OH2 and OH3), and the aldehyde group of D-xylose is stabilized by Asn306 through hydrogen bonding. The residues involved in formation of the D-xylose binding pocket are confirmed by site-directed mutagenesis experiments
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
D-xylose binding mode of SsXR is elucidated by molecular docking simulations of SsXR with the D-xylose substrate revealing that D-xylose fits well into the predicted substrate binding pocket. The D-xylose binding pocket consists of 10 residues: Trp20, Asp47, Trp79, His110, Phe111, Phe128, Phe221, Leu224, Asn306, and Trp311. The Asp47 residue contributes to the stabilization of two hydroxyl groups (OH2 and OH3), and the aldehyde group of D-xylose is stabilized by Asn306 through hydrogen bonding. The residues involved in formation of the D-xylose binding pocket are confirmed by site-directed mutagenesis experiments
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
D-xylose binding mode of SsXR is elucidated by molecular docking simulations of SsXR with the D-xylose substrate revealing that D-xylose fits well into the predicted substrate binding pocket. The D-xylose binding pocket consists of 10 residues: Trp20, Asp47, Trp79, His110, Phe111, Phe128, Phe221, Leu224, Asn306, and Trp311. The Asp47 residue contributes to the stabilization of two hydroxyl groups (OH2 and OH3), and the aldehyde group of D-xylose is stabilized by Asn306 through hydrogen bonding. The residues involved in formation of the D-xylose binding pocket are confirmed by site-directed mutagenesis experiments
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
kcat of wild-type enzyme increases by a factor of 1.73 when NADPH replaces NADH
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
using a modified iterative protein redesign and optimization workflow, a sets of mutations is identified that change the nicotinamide cofactor specificity of xylose reductase (CbXR) from its physiological preference for NADPH, to the alternate cofactor NADH
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
reaction is catalyzed by NADPH-dependent monospecific xylose reductase (msXR), and by dual specific xylose reductase (dsXR)
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
-
?
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
D-xylose reductase 1: 200% of the activity with D-xylose, D-xylose reductase 2: 268% of the activity with D-xylose, D-xylose reductase 3: 143% of the activity with D-xylose
-
-
?
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
D-xylose reductase 1: 200% of the activity with D-xylose, D-xylose reductase 2: 268% of the activity with D-xylose, D-xylose reductase 3: 143% of the activity with D-xylose
-
-
?
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
NADPH-dependent monospecific xylose reductase
-
-
?
L-arabinose + NADPH + H+
arabitol + NADP+
-
-
-
-
r
L-arabinose + NADPH + H+
arabitol + NADP+
-
-
-
r
L-arabinose + NADPH + H+
L-arabinitol + NADP+
-
D-xylose reductase 1: 117% of the activity with D-xylose, D-xylose reductase 2: 120% of the activity with D-xylose, D-xylose reductase 3: 101% of the activity with D-xylose
-
-
?
L-arabinose + NADPH + H+
L-arabinitol + NADP+
-
D-xylose reductase 1: 117% of the activity with D-xylose, D-xylose reductase 2: 120% of the activity with D-xylose, D-xylose reductase 3: 101% of the activity with D-xylose
-
-
?
L-arabinose + NADPH + H+
L-arabinitol + NADP+
79% of the activity with D-xylose
-
-
?
L-arabinose + NADPH + H+
L-arabinitol + NADP+
79% of the activity with D-xylose
-
-
?
L-arabinose + NADPH + H+
L-arabinitol + NADP+
-
NADPH-dependent monospecific xylose reductase
-
-
?
oenanthaldehyde + NADPH + H+
? + NADP+
-
-
-
-
?
oenanthaldehyde + NADPH + H+
? + NADP+
-
-
-
-
?
xylitol + NAD+
D-xylose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylose + NADH + H+
low activity with NAD(H)
-
-
r
xylitol + NAD+
D-xylose + NADH + H+
low activity with NAD(H)
-
-
r
xylitol + NADP+
D-xylose + NADPH + H+
-
-
-
r
xylitol + NADP+
D-xylose + NADPH + H+
-
-
-
r
xylitol + NADP+
D-xylose + NADPH + H+
-
-
-
r
xylitol + NADP+
D-xylose + NADPH + H+
-
-
-
r
xylitol + NADP+
D-xylose + NADPH + H+
-
-
-
-
r
additional information
?
-
-
specific activity analysis of Aspergillus niger XyrB shows that the enzyme is able to convert a wide range of sugars and polyols. XyrB shows the highest specific activity towards D-galactose, D-xylose and L-arabinose. The enzyme is also active with D-glucose, D-mannose, D-fructose, L-sorbose, D-ribose, D-arabinose, L-xylose, and L-rhamnose in the reductive reaction, and with ribitol, D-arabitol, sorbitol, mannitol, and glycerol in the oxidative reaction
-
-
-
additional information
?
-
analysis and comparison of activities of differently expressed recombinant enzymes in xylitol production through whole-cell catalysis from pure xylose and glucose
-
-
-
additional information
?
-
analysis and comparison of activities of differently expressed recombinant enzymes in xylitol production through whole-cell catalysis from pure xylose and glucose
-
-
-
additional information
?
-
the enzyme displays the highest catalytic efficiency for L-threose, followed by D-erythrose. DnXR exhibits broad substrate specificity, with the highest catalytic efficiency for C5 sugars like arabinose, xylose, and ribose and a strict preference for cosubstrate NADPH
-
-
-
additional information
?
-
Gre3 is generally described as aldose reductase, the enzyme is not particularly specific for xylose but has significant activity with other sugars, as well
-
-
-
additional information
?
-
Gre3 is generally described as aldose reductase, the enzyme is not particularly specific for xylose but has significant activity with other sugars, as well
-
-
-
additional information
?
-
the bottleneck of the enzyme activity in SsXR appears to be the binding affinity for D-xylose
-
-
-
additional information
?
-
-
the bottleneck of the enzyme activity in SsXR appears to be the binding affinity for D-xylose
-
-
-
additional information
?
-
the bottleneck of the enzyme activity in SsXR appears to be the binding affinity for D-xylose
-
-
-
additional information
?
-
the bottleneck of the enzyme activity in SsXR appears to be the binding affinity for D-xylose
-
-
-
additional information
?
-
the bottleneck of the enzyme activity in SsXR appears to be the binding affinity for D-xylose
-
-
-
additional information
?
-
the enzyme prefers NADPH as cofactor and shows broad substrate specificity, cf. EC 1.1.1.21. The enzyme is active with D-erythrose, D-ribose, D-arabinose, D-xylose, D-lyxose, D-allose, D-altrose, D-glucose, D-mannose, D-gulose, D-idose, and D-galactose. o activity with D-talose, fructose, sucrose, maltose, lactose, cellobiose, and xylobiose
-
-
-
additional information
?
-
the enzyme prefers NADPH as cofactor and shows broad substrate specificity, cf. EC 1.1.1.21. The enzyme is active with D-erythrose, D-ribose, D-arabinose, D-xylose, D-lyxose, D-allose, D-altrose, D-glucose, D-mannose, D-gulose, D-idose, and D-galactose. o activity with D-talose, fructose, sucrose, maltose, lactose, cellobiose, and xylobiose
-
-
-
additional information
?
-
in vitro the enzyme also catalyzes the reduction of ketones
-
-
?
additional information
?
-
analysis and comparison of activities of differently expressed recombinant enzymes in xylitol production through whole-cell catalysis from pure xylose and glucose
-
-
-
additional information
?
-
analysis and comparison of activities of differently expressed recombinant enzymes in xylitol production through whole-cell catalysis from pure xylose and glucose
-
-
-
additional information
?
-
-
Candida intermedia produces two isoforms of xylose reductase: one is NADPH-dependent (monospecific xylose reductase, msXR), and another prefers NADH about 4fold over NADPH (dual specific xylose reductase, dsXR)
-
-
-
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.
0.221
2-deoxy-D-galactose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.058
2-deoxy-D-glucose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.038
2-deoxy-D-ribose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
1.5 - 4.4
5,6-dideoxy-5,6-difluoro-D-glucofuranose
-
0.4 - 3
5,6-dideoxy-5-fluoro-D-glucofuranose
-
1 - 10.4
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose
-
0.9 - 2.2
5,6-dideoxy-D-xylo-hexofuranose
-
4
5-azido-5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
0.7 - 1
5-deoxy-D-xylofuranose
-
1 - 1.6
5-fluoro-5-deoxy-D-xylofuranose
-
0.6 - 1.3
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
-
1.8
benzaldehyde
pH 7.2, temperature not specified in the publication
2 - 3
Butanal
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.32 - 9.8
cyclohexanecarboxaldehyde
0.01
D-fucose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
1.14
DL-glyceraldehyde
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
4.2
furfural
pH 7.2, temperature not specified in the publication
0.117
L-Lyxose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.6 - 2.5
oenanthaldehyde
-
3.9
pentanal
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
78
propionaldehyde
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
additional information
additional information
-
1.5
5,6-dideoxy-5,6-difluoro-D-glucofuranose
-
pH 7, 25°C
-
4.4
5,6-dideoxy-5,6-difluoro-D-glucofuranose
-
pH 7, 25°C
-
0.4
5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
3
5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
1
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose
-
pH 7, 25°C
-
10.4
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose
-
pH 7, 25°C
-
0.9
5,6-dideoxy-D-xylo-hexofuranose
-
pH 7, 25°C
-
2.2
5,6-dideoxy-D-xylo-hexofuranose
-
pH 7, 25°C
-
0.7
5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
1
5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
1
5-fluoro-5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
1.6
5-fluoro-5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
0.6
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
1.3
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
0.32
cyclohexanecarboxaldehyde
-
pH 7, 25°C
9.8
cyclohexanecarboxaldehyde
-
pH 7, 25°C
0.033
D-erythrose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
5.5
D-erythrose
recombinant His-tagged enzyme, pH 7.0, 45°C
0.061
D-galactose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
51
D-galactose
-
pH 7, 25°C
72.2
D-galactose
pH 7.0, 30°C
303
D-galactose
-
pH 7, 25°C
0.006
D-glucose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
177
D-glucose
pH 7.0, 30°C
0.091
D-ribose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
36.3
D-ribose
pH 7.0, 30°C
0.016
D-xylose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.064
D-xylose
-
pH 7.2, 25°C
3.3
D-xylose
-
recombinant enzyme, pH 7.0, 25°C
14.8
D-xylose
-
pH 7.0, 22°C, wild-type enzyme
15.36
D-xylose
recombinant enzyme, pH 6.5, 50°C
28.1
D-xylose
pH 7.0, 30°C
30
D-xylose
-
pH 7.0, D-xylose reductase 2
32.37
D-xylose
with NADPH, without NaCl, pH 8.0, 30°C
34
D-xylose
-
pH 7.0, D-xylose reductase 3
37
D-xylose
-
pH 7.0, D-xylose reductase 1
39.4
D-xylose
with NADPH, with 150 mM NaCl, pH 8.0, 30°C
39.61
D-xylose
with NADH, without NaCl, pH 8.0, 30°C
59.72
D-xylose
with NADH, with 150 mM NaCl, pH 8.0, 30°C
81.8
D-xylose
-
pH 7.0, 25°C
160
D-xylose
pH 6.5, 35°C
258
D-xylose
pH 7.2, temperature not specified in the publication
0.02
L-arabinose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
9.9
L-arabinose
-
recombinant enzyme, pH 7.0, 25°C
41.7
L-arabinose
pH 7.0, 30°C
0.0187
NADH
without NaCl, pH 8.0, 30°C
0.136
NADH
with 150 mM NaCl, pH 8.0, 30°C
38
NADH
pH 7.0, 25°C, wild-type enzyme
40
NADH
pH 7.0, 25°C, mutant enzyme D50A
0.0073
NADPH
-
pH 7.0, 25°C
0.008
NADPH
-
30°C, cosubstrate: D-xylose or L-arabinose
0.009
NADPH
-
pH 7.0, D-xylose reductase 3
0.00928
NADPH
without NaCl, pH 8.0, 30°C
0.0094
NADPH
pH 7.0, 30°C
0.0095
NADPH
-
pH 7.2, 25°C
0.014
NADPH
-
pH 7.0, D-xylose reductase 1
0.018
NADPH
-
pH 7.0, D-xylose reductase 2
0.0277
NADPH
with 150 mM NaCl, pH 8.0, 30°C
2.3
NADPH
pH 7.0, 25°C, mutant enzyme D50A
3.2
NADPH
pH 7.0, 25°C, wild-type enzyme
7.6
NADPH
-
pH 7.0, 22°C, wild-type enzyme
0.6
oenanthaldehyde
-
pH 7, 25°C
-
2.5
oenanthaldehyde
-
pH 7, 25°C
-
334
xylitol
pH 7.0, 25°C, wild-type enzyme
537
xylitol
pH 7.0, 25°C, mutant enzyme D50A
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
KM-value determined with cell extract
-
additional information
additional information
-
comparison of kinetic constants of NADPH dependent D-xylose reductases and other pentose reductases from different fungal species, overview
-
additional information
additional information
Michaelis-Menten and Lineweaver-Burk plots by linear and nonlinear regression fitting
-
additional information
additional information
thermodynamics, recombinant enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8.4
2-deoxy-D-galactose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
6.8
2-deoxy-D-glucose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
1.4
2-deoxy-D-ribose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
19 - 22
5,6-dideoxy-5,6-difluoro-D-glucofuranose
-
14 - 21
5,6-dideoxy-5-fluoro-D-glucofuranose
-
14 - 34
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose
-
15 - 27
5,6-dideoxy-D-xylo-hexofuranose
-
11.2
5-azido-5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
12.5 - 18.1
5-deoxy-D-xylofuranose
-
15.6 - 20
5-fluoro-5-deoxy-D-xylofuranose
-
14 - 19
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
-
21.2
Butanal
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
6.3 - 13.1
cyclohexanecarboxaldehyde
20.7
D-fucose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
12.2
D-ribose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
24.3
DL-glyceraldehyde
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
18.4
L-Lyxose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
9.2 - 22
oenanthaldehyde
-
20.7
pentanal
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
6.9
propionaldehyde
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
19
5,6-dideoxy-5,6-difluoro-D-glucofuranose
-
pH 7, 25°C
-
22
5,6-dideoxy-5,6-difluoro-D-glucofuranose
-
pH 7, 25°C
-
14
5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
21
5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
14
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose
-
pH 7, 25°C
-
34
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose
-
pH 7, 25°C
-
15
5,6-dideoxy-D-xylo-hexofuranose
-
pH 7, 25°C
-
27
5,6-dideoxy-D-xylo-hexofuranose
-
pH 7, 25°C
-
12.5
5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
18.1
5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
15.6
5-fluoro-5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
20
5-fluoro-5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
14
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
19
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
6.3
cyclohexanecarboxaldehyde
-
pH 7, 25°C
13.1
cyclohexanecarboxaldehyde
-
pH 7, 25°C
24.3
D-erythrose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
165
D-erythrose
recombinant His-tagged enzyme, pH 7.0, 45°C
420
D-fructose
pH 5.0, 30°C, recombinant engineered Pir-XR enzyme
466
D-fructose
pH 5.0, 30°C, recombinant wild-type enzyme
530
D-fructose
pH 5.0, 30°C, recombinant engineered XR-GPI enzyme
5.9
D-galactose
-
pH 7, 25°C
9.4
D-galactose
-
pH 7, 25°C
15.2
D-galactose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
350
D-galactose
pH 5.0, 30°C, recombinant engineered Pir-XR enzyme
360
D-galactose
pH 5.0, 30°C, recombinant wild-type enzyme
410
D-galactose
pH 5.0, 30°C, recombinant engineered XR-GPI enzyme
8.2
D-glucose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
790
D-glucose
pH 5.0, 30°C, recombinant wild-type enzyme
1920
D-glucose
pH 5.0, 30°C, recombinant engineered Pir-XR enzyme
3190
D-glucose
pH 5.0, 30°C, recombinant engineered XR-GPI enzyme
2 - 8
D-xylose
-
pH 7, 25°C
3.02
D-xylose
with NADH, with 150 mM NaCl, pH 8.0, 30°C
4.34
D-xylose
with NADH, without NaCl, pH 8.0, 30°C
6.69
D-xylose
with NADPH, with 150 mM NaCl, pH 8.0, 30°C
8.37
D-xylose
with NADPH, without NaCl, pH 8.0, 30°C
8.8
D-xylose
-
pH 7, 25°C
9.65
D-xylose
-
recombinant enzyme, pH 7.0, 25°C
13.1
D-xylose
-
pH 7.0, 22°C, wild-type enzyme
14.6
D-xylose
-
pH 7, 25°C
21.3
D-xylose
pH 7.0, 30°C
23.5
D-xylose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
157
D-xylose
pH 5.0, 30°C, recombinant wild-type enzyme
194.3
D-xylose
recombinant enzyme, pH 6.5, 50°C
227
D-xylose
pH 5.0, 30°C, recombinant engineered Pir-XR enzyme
343
D-xylose
pH 5.0, 30°C, recombinant engineered XR-GPI enzyme
4638
D-xylose
-
pH 6.3, 25°C
15.61
L-arabinose
-
recombinant enzyme, pH 7.0, 25°C
24.5
L-arabinose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
900
L-arabinose
pH 5.0, 30°C, recombinant engineered XR-GPI enzyme
1000
L-arabinose
pH 5.0, 30°C, recombinant engineered Pir-XR enzyme
1030
L-arabinose
pH 5.0, 30°C, recombinant wild-type enzyme
2.39
NADH
with 150 mM NaCl, pH 8.0, 30°C
2.68
NADH
without NaCl, pH 8.0, 30°C
0.06
NADPH
pH 5.0, 30°C, recombinant wild-type enzyme
0.14
NADPH
pH 5.0, 30°C, recombinant engineered XR-GPI enzyme
0.17
NADPH
pH 5.0, 30°C, recombinant engineered Pir-XR enzyme
7.63
NADPH
with 150 mM NaCl, pH 8.0, 30°C
7.65
NADPH
without NaCl, pH 8.0, 30°C
9.2
oenanthaldehyde
-
pH 7, 25°C
-
22
oenanthaldehyde
-
pH 7, 25°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.7 - 38
2-deoxy-D-galactose
117
2-deoxy-D-glucose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
36.8
2-deoxy-D-ribose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
4.32 - 14.67
5,6-dideoxy-5,6-difluoro-D-glucofuranose
-
7 - 35
5,6-dideoxy-5-fluoro-D-glucofuranose
-
3.27 - 14
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose
-
12.27 - 16.67
5,6-dideoxy-D-xylo-hexofuranose
-
1.12 - 2.8
5-azido-5-deoxy-D-xylofuranose
-
17.86 - 18.1
5-deoxy-D-xylofuranose
-
12.5 - 15.6
5-fluoro-5-deoxy-D-xylofuranose
-
14.62 - 23.33
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
-
0.2 - 0.9
6-azido-5,6-dideoxy-D-xylo-hexofuranose
-
0.93
Butanal
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.64 - 40.94
cyclohexanecarboxaldehyde
2070
D-fucose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
134
D-ribose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.3 - 21.3
DL-glyceraldehyde
157
L-Lyxose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
138
L-threose
recombinant His-tagged enzyme, pH 7.0, 45°C
8.8 - 15.33
oenanthaldehyde
-
5.31
pentanal
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.09
propionaldehyde
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.0013
xylitol
-
pH 7, 25°C
3.7
2-deoxy-D-galactose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309D, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
6.3
2-deoxy-D-galactose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme D50A, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
9.3
2-deoxy-D-galactose
pH 7.0, 25°C, cofactor: NADH, wild-type enzyme, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
17
2-deoxy-D-galactose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309A, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
38
2-deoxy-D-galactose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
4.32
5,6-dideoxy-5,6-difluoro-D-glucofuranose
-
pH 7, 25°C
-
14.67
5,6-dideoxy-5,6-difluoro-D-glucofuranose
-
pH 7, 25°C
-
7
5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
35
5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
3.27
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose
-
pH 7, 25°C
-
14
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose
-
pH 7, 25°C
-
12.27
5,6-dideoxy-D-xylo-hexofuranose
-
pH 7, 25°C
-
16.67
5,6-dideoxy-D-xylo-hexofuranose
-
pH 7, 25°C
-
1.12
5-azido-5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
2.8
5-azido-5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
17.86
5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
18.1
5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
12.5
5-fluoro-5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
15.6
5-fluoro-5-deoxy-D-xylofuranose
-
pH 7, 25°C
-
14.62
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
23.33
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
-
pH 7, 25°C
-
0.2
6-azido-5,6-dideoxy-D-xylo-hexofuranose
-
pH 7, 25°C
-
0.9
6-azido-5,6-dideoxy-D-xylo-hexofuranose
-
pH 7, 25°C
-
0.64
cyclohexanecarboxaldehyde
-
pH 7, 25°C
40.94
cyclohexanecarboxaldehyde
-
pH 7, 25°C
30
D-erythrose
recombinant His-tagged enzyme, pH 7.0, 45°C
736
D-erythrose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.03
D-galactose
-
pH 7, 25°C
0.116
D-galactose
-
pH 7, 25°C
5.5
D-galactose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309D, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
9
D-galactose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309A, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
70
D-galactose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme D50A, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
249
D-galactose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
265
D-galactose
pH 7.0, 25°C, cofactor: NADH, wild-type enzyme, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
8.3
D-glucose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309A, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
8.3
D-glucose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309D, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
188
D-glucose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme D50A, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
833
D-glucose
pH 7.0, 25°C, cofactor: NADH, wild-type enzyme, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
1370
D-glucose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.051
D-xylose
with NADH, with 150 mM NaCl, pH 8.0, 30°C
0.11
D-xylose
with NADH, without NaCl, pH 8.0, 30°C
0.17
D-xylose
with NADPH, with 150 mM NaCl, pH 8.0, 30°C
0.18
D-xylose
-
pH 7, 25°C
0.259
D-xylose
with NADPH, without NaCl, pH 8.0, 30°C
0.33
D-xylose
-
pH 7, 25°C
0.36
D-xylose
-
pH 7, 25°C
0.89
D-xylose
-
pH 7.0, 22°C, wild-type enzyme
2.92
D-xylose
-
recombinant enzyme, pH 7.0, 25°C
6.5
D-xylose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme W23Y, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose
9
D-xylose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309D, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose
12.65
D-xylose
recombinant enzyme, pH 6.5, 50°C
14
D-xylose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme D50A, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose
19
D-xylose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309A, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose
25
D-xylose
pH 7.0, 25°C, cofactor: NADH, mutant enzyme W23F, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose
680
D-xylose
pH 7.0, 25°C, cofactor: NADH, wild-type enzyme, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose
1470
D-xylose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.3
DL-glyceraldehyde
pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309A, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
0.3
DL-glyceraldehyde
pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309D, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
8.9
DL-glyceraldehyde
pH 7.0, 25°C, cofactor: NADH, wild-type enzyme, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose
21.3
DL-glyceraldehyde
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
1.58
L-arabinose
-
recombinant enzyme, pH 7.0, 25°C
1230
L-arabinose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
17.57
NADH
with 150 mM NaCl, pH 8.0, 30°C
143.3
NADH
without NaCl, pH 8.0, 30°C
240
NADPH
-
pH 7, 25°C
275.5
NADPH
with 150 mM NaCl, pH 8.0, 30°C
824.4
NADPH
without NaCl, pH 8.0, 30°C
8.8
oenanthaldehyde
-
pH 7, 25°C
-
15.33
oenanthaldehyde
-
pH 7, 25°C
-
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evolution
-
D-xylose reductase is a member of the aldo-keto reductase family. Its catalytic mechanism is likely conserved in other AKRs that contain these amino acids. Expression profiles for D-xylose reductase xyrA, D-xylose reductase xyrB and L-arabinose reductase larA from Aspergillus niger, overview
evolution
phylogenetic tree analysis, overview
evolution
the xylose reductase (XR) belongs to the AKR2 family xylose reductase of aldo-keto reductase (AKR) superfamily
evolution
-
phylogenetic tree analysis, overview
-
evolution
-
phylogenetic tree analysis, overview
-
evolution
-
phylogenetic tree analysis, overview
-
malfunction
alteration in both secondary and tertiary structures cause enzyme deactivation in acidic pH, while increased deactivation rates at alkaline pH are attributed to the variation of tertiary structure over time
malfunction
-
expression of gene xyrB is strongly reduced in the xlnR deletion strain on D-xylose and in the araR deletion strain on L-arabinose, indicating control of its expression by both regulators
malfunction
-
alteration in both secondary and tertiary structures cause enzyme deactivation in acidic pH, while increased deactivation rates at alkaline pH are attributed to the variation of tertiary structure over time
-
metabolism
the redox balance between xylose reductase (XR) and xylitol dehydrogenase (XDH, EC 1.1.1.10) is thought to be an important factor in effective xylose fermentation
metabolism
biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH, EC 1.1.1.9). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
metabolism
-
D-xylose reductase is involved in D-xylose and L-arabinose conversion through the pentose catabolic pathway (PCP) in fungi
metabolism
enzyme XR is the first enzyme in the xylose utilization pathway. Debaryomyces nepalensis, a nonpathogenic Saccharomycetes yeast can utilize both hexose and pentose sugars to produce polyols. DnXR is a key metabolic enzyme in the D-xylose utilization pathway
metabolism
-
derivatives of D-xylose and D-glucose, in which the hydroxy groups at C-5, and C-5 and C-6 are replaced by fluorine, hydrogen and azide are reduced with up to 3000fold increased catalytic efficiencies. Azide introduced at C-5 or C-6 destabilizes the transition state of reduction of the corresponding hydrogen-substituted aldoses by approx. 4 kJ/mol
metabolism
-
derivatives of D-xylose and D-glucose, in which the hydroxy groups at C-5, and C-5 and C-6 are replaced by fluorine, hydrogen and azide are reduced with up to 3000fold increased catalytic efficiencies. Azide introduced at C-5 or C-6 destabilizes the transition state of reduction of the corresponding hydrogen-substituted aldoses by approx. 4 kJ/mol
metabolism
-
ordered mechanism in which coenzyme binds first and substrate second
physiological function
strictly NADPH-dependent xylose reductase with mutated strict NADP+-dependent xylitol dehydrogenase, EC 1.1.1.10, are more effective in increasing bioethanol production and decreasing xylitol accumulation than the wild-type, overview
physiological function
xylitol production through whole-cell catalysis from pure xylose and glucose, and xylitol production from cornstalk hydrolysate
physiological function
xylitol production through whole-cell catalysis from pure xylose and glucose, and xylitol production from cornstalk hydrolysate, method optimization, overview
physiological function
xylose reductase is a key enzyme in the conversion of xylose to xylitol, it catalyzes the conversion of carbonyl substrates into their respective alcohols
physiological function
-
an enzyme mutant shows poor growth on D-xylose but normal growth on xylitol and D-glucose. Growth rate, growth yield, and D-xylose consumption rate of the mutant are less sensitive than those of the wild-type to changes in aeration rate. D-Xylose is utilized more efficiently in that less of a by-product, xylitol, is produced
physiological function
-
Candida intermedia produces two different isoforms. Isoform I is strictly specific for NADPH, isoform II shows similar specificity constants for NADPH and NADH
physiological function
-
D-xylose, L-arabinose and D-galactose serve as substrates for NADPH-linked reactions in extracts of cells grown in medium containing D-xylose, L-arabinose, or D-galactose. Xylitol, L-arabitol, and galactitol are the respective conversion products of these sugars
physiological function
-
deletion of the XyrB gene in the D-xylose reductase/L-arabinose reductase LarA/XyrA deletion background completely abolishes growth on both pentoses. This mutant does not accumulate any pathway intermediates but accumulates high amounts of L-arabinose and D-xylose when grown on these sugars
physiological function
-
isoform ALR1 is strictly specific for NADPH, EC 1.1.1.431, whereas isoform ALR2 utilises NADH and NADPH with similar specificity constants, EC 1.1.1.307
physiological function
-
xylitol production through whole-cell catalysis from pure xylose and glucose, and xylitol production from cornstalk hydrolysate
-
physiological function
-
xylitol production through whole-cell catalysis from pure xylose and glucose, and xylitol production from cornstalk hydrolysate, method optimization, overview
-
additional information
structure-function analysis, molecular docking simulation, overview. The SsXR structure in complex with the NADPH cofactor shows that the protein undergoes an open/closed conformation change upon NADPH binding. The substrate binding pocket of SsXR is somewhat hydrophobic, which seems to result in low binding affinity to the substrate. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
additional information
-
structure-function analysis, molecular docking simulation, overview. The SsXR structure in complex with the NADPH cofactor shows that the protein undergoes an open/closed conformation change upon NADPH binding. The substrate binding pocket of SsXR is somewhat hydrophobic, which seems to result in low binding affinity to the substrate. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
additional information
the catalytic site architecture of AKRs includes a highly conserved tetrad of residues Asp42, Tyr47, Lys76, and His109 (DnXR numbering) lining the bottom of a deep open cavity
additional information
-
the enzyme contains an aldo/keto reductase (AKR) motif between positions 22-277. The mechanism of catalysis in AKRs involves a catalytic tetrad, His, Tyr, Lys and Asp, in which the tyrosine hydroxyl group is the general acid and appears to be a proton relay from the histidine or lysine
additional information
-
structure-function analysis, molecular docking simulation, overview. The SsXR structure in complex with the NADPH cofactor shows that the protein undergoes an open/closed conformation change upon NADPH binding. The substrate binding pocket of SsXR is somewhat hydrophobic, which seems to result in low binding affinity to the substrate. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
-
additional information
-
structure-function analysis, molecular docking simulation, overview. The SsXR structure in complex with the NADPH cofactor shows that the protein undergoes an open/closed conformation change upon NADPH binding. The substrate binding pocket of SsXR is somewhat hydrophobic, which seems to result in low binding affinity to the substrate. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
-
additional information
-
structure-function analysis, molecular docking simulation, overview. The SsXR structure in complex with the NADPH cofactor shows that the protein undergoes an open/closed conformation change upon NADPH binding. The substrate binding pocket of SsXR is somewhat hydrophobic, which seems to result in low binding affinity to the substrate. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
-
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?
-
x * 33470, about, sequence calculation
?
-
x * 36300, calculated
-
?
x * 35000, recombinant enzyme, SDS-PAGE
?
-
x * 37000, wild-type and mutant enzyme Y49F, SDS-PAGE
dimer
-
2 * 364978, D-xylose reductase 1, ion-spray mass spectrometry
dimer
-
2 * 365540, D-xylose reductase 2, ion-spray mass spectrometry
dimer
-
2 * 364978, D-xylose reductase 1, ion-spray mass spectrometry
-
dimer
-
2 * 365540, D-xylose reductase 2, ion-spray mass spectrometry
-
dimer
-
2 * 29000, SDS-PAGE
dimer
2 * 36724, calculated, 2 * 38000, SDS-PAGE
dimer
-
2 * 36724, calculated, 2 * 38000, SDS-PAGE
-
dimer
-
2 * 36000, SDS-PAGE, 2 * 35823, MALDI-TOF
homodimer
-
monomer
x * 39200, recombinant enzyme, SDS-PAGE, x * 36740, sequence calculation
monomer
-
x * 39200, recombinant enzyme, SDS-PAGE, x * 36740, sequence calculation
-
monomer or dimer
x * 37500, about
monomer or dimer
-
x * 37500, about
-
monomer or dimer
-
x * 37500, about
-
monomer or dimer
-
x * 37500, about
-
additional information
two SsXR polypeptide chains in an asymmetric unit form a dimer. SsXR generally separated into monomers in 50 and 100 mM NaCl and completely separated into monomers in150 mM NaCl, although it exists as dimers in the absence of NaCl. Based on these results, it is suggested that SsXR exists as a monomer under the physiological NaCl concentration and tends to form a dimer in the presence of low NaCl concentrations. Oligomer formation affects enzyme activity. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
additional information
-
two SsXR polypeptide chains in an asymmetric unit form a dimer. SsXR generally separated into monomers in 50 and 100 mM NaCl and completely separated into monomers in150 mM NaCl, although it exists as dimers in the absence of NaCl. Based on these results, it is suggested that SsXR exists as a monomer under the physiological NaCl concentration and tends to form a dimer in the presence of low NaCl concentrations. Oligomer formation affects enzyme activity. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
additional information
-
two SsXR polypeptide chains in an asymmetric unit form a dimer. SsXR generally separated into monomers in 50 and 100 mM NaCl and completely separated into monomers in150 mM NaCl, although it exists as dimers in the absence of NaCl. Based on these results, it is suggested that SsXR exists as a monomer under the physiological NaCl concentration and tends to form a dimer in the presence of low NaCl concentrations. Oligomer formation affects enzyme activity. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
-
additional information
-
two SsXR polypeptide chains in an asymmetric unit form a dimer. SsXR generally separated into monomers in 50 and 100 mM NaCl and completely separated into monomers in150 mM NaCl, although it exists as dimers in the absence of NaCl. Based on these results, it is suggested that SsXR exists as a monomer under the physiological NaCl concentration and tends to form a dimer in the presence of low NaCl concentrations. Oligomer formation affects enzyme activity. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
-
additional information
-
two SsXR polypeptide chains in an asymmetric unit form a dimer. SsXR generally separated into monomers in 50 and 100 mM NaCl and completely separated into monomers in150 mM NaCl, although it exists as dimers in the absence of NaCl. Based on these results, it is suggested that SsXR exists as a monomer under the physiological NaCl concentration and tends to form a dimer in the presence of low NaCl concentrations. Oligomer formation affects enzyme activity. The monomeric structure of SsXR is composed of 15 alpha-helices (alpha1-alpha15) and 10 beta-strands (beta1-beta10). The monomeric structure of SsXR consists of a core domain and two auxiliary regions (ARs), AR-I and AR-II. The core domain consists of 13 alpha-helices (alpha1-alpha10, alpha12-alpha13, and alpha15) and eight beta-strands (beta3-beta10) and forms a TIM-barrel motif. As the conventional TIM-barrel motif, in SsXR eight parallel beta-strands (beta3-beta10) are arranged in a cylindrical shape with eight surrounding alpha-helices (alpha1, alpha3, alpha5-alpha8, and alpha12-alpha13). Four alpha-helices (alpha2, alpha9-alpha10, and alpha15) are located at the back of the TIM-barrel motif and contribute to binding of the NADPH cofactor. AR-I is composed of two beta-strands (beta1-beta2) and is located on the opposite side of the TIM-barrel. AR-II consists of two alpha-helices (alpha11 and alpha14) and is positioned next to the alpha12 helix. As reported in other enzymes belonging to AKR families, four catalytic residues, Asp43, Tyr48, Lys77, and His110, are also conserved in the SsXR, and involved in the catalytic mechanism
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Y49F
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more than 98% loss of activity compared to wild-type enzyme
D47A
site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
F111A
site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
F128A
site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
F221A
site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
H110A
site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
K21A
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mutation reverses the cofactor specificity from major NADP- to NAD-dependent
K270N
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mutation reverses the cofactor specificity from major NADP- to NAD-dependent
L224A
site-directed mutagenesis of the substrate binding residue, the mutant shows 35% XR activity compared to the wild-type enzyme
N306A
site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
W20A
site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
W311A
site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
W79A
site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
D47A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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F221A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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H110A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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L224A
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site-directed mutagenesis of the substrate binding residue, the mutant shows 35% XR activity compared to the wild-type enzyme
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N306A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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D47A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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F221A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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H110A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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L224A
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site-directed mutagenesis of the substrate binding residue, the mutant shows 35% XR activity compared to the wild-type enzyme
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N306A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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D47A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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F221A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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H110A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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L224A
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site-directed mutagenesis of the substrate binding residue, the mutant shows 35% XR activity compared to the wild-type enzyme
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N306A
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site-directed mutagenesis of the substrate binding residue, the mutant shows almost complete loss of activity
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D50A
mutant shows 31% and 18% of the wild-type catalytic-centre activities for xylose reduction and xylitol oxidation respectively, consistent with a decrease in the rates of the chemical steps caused by the mutation, but no change in the apparent substrate binding constants and the pattern of substrate specificities
N309A
the 30fold preference of the wild-type for D-galactose compared with 2-deoxy-D-galactose is lost completely in the mutant. Replacement of Asn309 with alanine or aspartic acid disrupts the function of the original side chain in donating a hydrogen atom for bonding with the substrate C-2(R) hydroxy group, thus causing a loss of transition-state stabilization energy of 89 kJ/mol
N309D
the 30fold preference of the wild-type for D-galactose compared with 2-deoxy-D-galactose is lost completely in the mutant. Comparison of the 2.4 A X-ray crystal structure of mutant N309D bound to NAD+ with the previous structure of the wild-type holoenzyme reveals no major structural perturbations. Replacement of Asn309 with alanine or aspartic acid disrupts the function of the original side chain in donating a hydrogen atom for bonding with the substrate C-2(R) hydroxy group, thus causing a loss of transition-state stabilization energy of 89 kJ/mol
W23F
mutant catalyses NADH-dependent reduction of xylose with 4% of the wild-type efficiency (kcat/Km), but improves the wild-type selectivity for utilization of ketones, relative to xylose, by factors of 156
W23Y
mutant catalyses NADH-dependent reduction of xylose with 1% of the wild-type efficiency (kcat/Km), but improves the wild-type selectivity for utilization of ketones, relative to xylose, by factors of 471
K274R
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mutation introduced to change the specificity toward NADH. Fermentation with the mutant strain shows a 2.8fold reduction in xylitol accumulation and 4.5fold increase in citric acid production compared to the wild-type strain
K274R
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mutation introduced to change the specificity toward NADH. Fermentation with the mutant strain shows a 2.8fold reduction in xylitol accumulation and 4.5fold increase in citric acid production compared to the wild-type strain
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K274R/N276D
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structure-guided site-directed mutagenesis, change of the coenzyme preference of the xyluose reductase about 170fold from NADPH in the wild-type to NADH, which, in spite of the structural modifications introduced, has retained the original catalytic efficiency for reduction of xylose by NADH
K274R/N276D
NADH-specific mutant, Saccharomyces cerevisiae expressing mutant K274R/N276D exhibits intracellular activities of 0.94 U/mg 1.07 U/mg with NADPH and NADH, respectively
additional information
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production of xylitol from D-xylose and D-glucose with recombinant Corynebacterium glutamicum, the strain is engineered to express the xylose reductase gene XYL1of Pichia stipitis, and produces xylose reductase with a specific activity of ca. 0.6 U/mg protein. Due to the absence of xylose isomerase and xylitol dehydrogenase genes, loose catabolite repression, high NADPH regeneration capacity, and tolerance against sugar-induced osmotic stress, the recombinant biocatalyst is able to efficiently produce xylitol from D-xylose using glucose as source of reducing equivalents
additional information
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production of xylitol from D-xylose and D-glucose with recombinant Corynebacterium glutamicum, the strain is engineered to express the xylose reductase gene XYL1of Pichia stipitis, and produces xylose reductase with a specific activity of ca. 0.6 U/mg protein. Due to the absence of xylose isomerase and xylitol dehydrogenase genes, loose catabolite repression, high NADPH regeneration capacity, and tolerance against sugar-induced osmotic stress, the recombinant biocatalyst is able to efficiently produce xylitol from D-xylose using glucose as source of reducing equivalents
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additional information
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the native xylose reductase gene Kmxyl1 of the Kluyveromyces marxianus strain YHJ010 is substituted with xylose reductase or its mutants N272D, K21A/N272D, or K270M from Pichia stipitis, i.e. Scheffersomyces stipitis, resulting in Kluyveromyces marxianus strains YZB013, YZB014, and YZB015. The ability of the resultant recombinant strains to assimilate xylose to produce xylitol and ethanol at elevated temperature is greatly improved, overview. But the strain YZB015 expressing a mutant PsXR K21A/N272D, with which co-enzyme preference is completely reversed from NADPH to NADH, fails to ferment due to the low expression
additional information
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the native xylose reductase gene Kmxyl1 of the Kluyveromyces marxianus strain YHJ010 is substituted with xylose reductase or its mutants N272D, K21A/N272D, or K270M from Pichia stipitis, i.e. Scheffersomyces stipitis, resulting in Kluyveromyces marxianus strains YZB013, YZB014, and YZB015. The ability of the resultant recombinant strains to assimilate xylose to produce xylitol and ethanol at elevated temperature is greatly improved, overview. But the strain YZB015 expressing a mutant PsXR K21A/N272D, with which co-enzyme preference is completely reversed from NADPH to NADH, fails to ferment due to the low expression
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additional information
efficient biosynthesis of xylitol from xylose by coexpression of xylose reductase (XR) from Rhizopus oryzae and glucose dehydrogenase (GDH) from Exiguobacterium sibiricum, the latter is used for cofactor regeneration, in Escherichia coli strain BL21(DE3)/pCDFDuet-1-XR-GDH, from Escherichia coli strains BL21(DE3)/pET28b(+)-XR and BL21(DE3)/pET28b(+)-GDH. The xylitol yield of the coupled system is maximal at pH 8.0 and 30°C, and at a unit ratio of GDH to XR concentration of 4:1, indicating that the regeneration of coenzyme had a significant effect on xylitol synthesis. Method optimization, overview
additional information
the enzyme is labelled by the insertion of the hemagglutinin (HA) tag between the end of the secretion signal sequence and the original XR. The obtained proteinis designated as XR-GPI. The second construct is obtained by fusing Pir4/Ccw5 protein to the N-terminus of XR and the addition of the HA tag to the C-terminus of the construct. This protein is named Pir-XR
additional information
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the enzyme is labelled by the insertion of the hemagglutinin (HA) tag between the end of the secretion signal sequence and the original XR. The obtained proteinis designated as XR-GPI. The second construct is obtained by fusing Pir4/Ccw5 protein to the N-terminus of XR and the addition of the HA tag to the C-terminus of the construct. This protein is named Pir-XR
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additional information
construction of a set of recombinant Saccharomyces cerevisiae carrying a mutated strictly NADPH-dependent xylose reductase and NADP+-dependent xylitol dehydrogenase 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
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construction of a set of recombinant Saccharomyces cerevisiae carrying a mutated strictly NADPH-dependent xylose reductase and NADP+-dependent xylitol dehydrogenase 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
enzyme XRTL can therefore be used in a cell-free xylitol production process or as part of a pathway for utilization of xylose from lignocellulosic waste. Ferulic acid is an inhibitor of the lignocellulosic activity
additional information
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enzyme XRTL can therefore be used in a cell-free xylitol production process or as part of a pathway for utilization of xylose from lignocellulosic waste. Ferulic acid is an inhibitor of the lignocellulosic activity
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additional information
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the mutant Candida tenuis enzyme is modified in its cofactor specificity showing preference for NADPH compared to NADH in the D-xylose reduction reaction, genetic metabolic engineering for improvement of xylose metabolism and fermentation in wild-type Saccharomyces cerevisiae strains, which are not able to naturally metabolize D-xylulose, overview
additional information
efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview
additional information
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efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview
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