1.1.1.431: D-xylose reductase (NADPH)
This is an abbreviated version!
For detailed information about D-xylose reductase (NADPH), go to the full flat file.
Reaction
Synonyms
ALR1, Cb-XR, CbXR, CtXR, D-xylose reductase, D-xylose reductase 1, D-xylose reductase 2, D-xylose reductase 3, DnXR, GRE3, monospecific xylose reductase, More, msXR, NAD(P)H-dependent D-xylose reductase, NAD(P)H-dependent xylose reductase, NADPH dependent D-xylose reductase, NADPH-dependent D-xylose reductase II,III, NADPH-dependent xylose reductase, NADPH-preferring xylose reductase, NRRL3_10868, SsXR, Texr, TrxR, XR1, XR2, XR3, XRTL, XYL1, xylose reductase, xyr8, XyrA, XyrB
ECTree
1.1.1.431 D-xylose reductase (NADPH)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.1.1.431 - D-xylose reductase (NADPH)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-hydroxymethylfurfural + NADH + H+
(furan-2,5-diyl)dimethanol + NAD+
low activity
-
-
r
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
best substrate
-
-
r
butanal + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-erythrose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-fucose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-galactose + NADH + H+
?
48% of the activity compared to D-xylose (with NADH as cofactor)
-
-
?
D-glucose + NADH + H+
?
10 of the activity compared to D-xylose (with NADH as cofactor)
-
-
?
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
-
-
?
furfural + NADH + H+
(furan-2-yl)methanol + NAD+
-
-
-
r
L-lyxose + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
pentanal + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
propionaldehyde + NADPH + H+
?
-
NADPH-dependent monospecific xylose reductase
-
-
?
5,6-dideoxy-5,6-difluoro-D-glucofuranose + NADPH + H+
? + NADP+
-
-
-
-
?
5,6-dideoxy-6-fluoro-D-xylo-hexofuranose + 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+
-
-
-
-
?
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+
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-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)+
-
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)+
-
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)+
-
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 + NADH + H+
xylitol + NAD+
NADPH is the preferred cofactor
-
-
?
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+
-
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+
-
kinetic mechanism of xylose reductase is iso-ordered bi bi
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
NADPH is the preferred cofactor, specific for D-xylose
-
-
?
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+
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+
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+
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+
kcat of wild-type enzyme increases by a factor of 1.73 when NADPH replaces NADH
-
-
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+
-
reaction is catalyzed by NADPH-dependent monospecific xylose reductase (msXR), and by dual specific xylose reductase (dsXR)
-
-
?
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+
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
-
-
?
xylitol + NAD+
D-xylose + NADH + H+
low activity with NAD(H)
-
-
r
xylitol + NAD+
D-xylose + NADH + H+
low activity with NAD(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
?
-
Yamadazyma tenuis CBS 4435
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)
-
-
-
