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Information on EC 1.1.1.431 - D-xylose reductase (NADPH)
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1.1.1.431 D-xylose reductase (NADPH)IUBMB Comments
Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH (e.g. the enzymes from Saccharomyces cerevisiae, Aspergillus niger, Trichoderma reesei, Candida tropicalis, Saitozyma flava, and Candida intermedia). Some D-xylose reductases have dual coenzyme specificity, though they still prefer NADPH to NADH (cf. EC 1.1.1.307, D-xylose reductase [NAD(P)H]). Very rarely the enzyme prefers NADH (cf. EC 1.1.1.430, D-xylose reductase (NADH)).
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
d-xylose reductase, nadph-dependent xylose reductase, d-xylose reductase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CtXR
D-xylose reductase 1
D-xylose reductase 2
D-xylose reductase 3
DnXR
GRE3
msXR
NAD(P)H-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
XRTL
XYL1
xylose reductase
xyr8
XyrA
XyrB
additional information
msXR
-
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, cf. 1.1.1.430)
XYL1
-
-
-
-
XYL1
-
-
ambiguous
-
XyrA
-
-
-
-
XyrB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+
structure-function analysis, overview
xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+
-
-
-
-
xylitol + NADP+ = D-xylose + NADPH + H+
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-
-
-
xylitol + NADP+ = D-xylose + NADPH + H+
kinetic mechanism of xylose reductase is iso-ordered bi bi
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PATHWAY SOURCE
PATHWAYS
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-
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SYSTEMATIC NAME
IUBMB Comments
xylitol:NADP+ oxidoreductase
Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH (e.g. the enzymes from Saccharomyces cerevisiae, Aspergillus niger, Trichoderma reesei, Candida tropicalis, Saitozyma flava, and Candida intermedia). Some D-xylose reductases have dual coenzyme specificity, though they still prefer NADPH to NADH (cf. EC 1.1.1.307, D-xylose reductase [NAD(P)H]). Very rarely the enzyme prefers NADH (cf. EC 1.1.1.430, D-xylose reductase (NADH)).
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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