Information on EC 1.1.1.307 - D-xylose reductase

for references in articles please use BRENDA:EC1.1.1.307
Word Map on EC 1.1.1.307
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.307
-
RECOMMENDED NAME
GeneOntology No.
D-xylose reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+
show the reaction diagram
xylitol + NAD+ = D-xylose + NADH + H+
show the reaction diagram
xylitol + NADP+ = D-xylose + NADPH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pentose and glucuronate interconversions
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD(P)+ oxidoreductase
Xylose reductase catalyses the initial reaction in the xylose utilization pathway, the NAD(P)H dependent reduction of xylose to xylitol.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
KFCC-10875
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
IF0 0618
-
-
Manually annotated by BRENDA team
SCTCC 300249
UniProt
Manually annotated by BRENDA team
gene XYL1
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Torulopsis molishiama
-
-
-
Manually annotated by BRENDA team
Torulopsis molishiama 55
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
ssp. mobilis, and strain A3, an engineered strain ZM4 that is adapted to 5% D-xylose, gene ZMO0976
UniProt
Manually annotated by BRENDA team
ssp. mobilis, and strain A3, an engineered strain ZM4 that is adapted to 5% D-xylose, gene ZMO0976
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4'-dichloroacetophenone + NADH + H+
? + NAD+
show the reaction diagram
-
binding and transformation of unnatural 2,4-dichloroacetophenone is not as for good as natural substrates, although it is reduced with very high catalytic efficiency
-
-
?
2-deoxy-D-galactose + NADH
?
show the reaction diagram
-
-
-
?
2-deoxy-D-galactose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
2-deoxy-D-galactose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
2-deoxy-D-glucose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
2-deoxy-D-ribose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
2-deoxy-D-ribose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
5-hydroxymethylfurfural + NADH + H+
(furan-2,5-diyl)dimethanol + NAD+
show the reaction diagram
9,10-phenanthrenequinone + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
show the reaction diagram
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
show the reaction diagram
butanal + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
butanal + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-arabinose + NADPH + H+
?
show the reaction diagram
D-arabinose + NADPH + H+
D-arabinitol + NADP+
show the reaction diagram
D-erythrose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
D-erythrose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-erythrose + NADPH + H+
D-erythritol + NADP+
show the reaction diagram
D-erythrose + NADPH + H+
erythritol + NADP+
show the reaction diagram
-
catalytic efficiency is 100fold higher than the catalytic efficiency for D-xylose
-
-
?
D-fucose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
D-fucose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-galactose + NADH
?
show the reaction diagram
-
-
-
?
D-galactose + NADH + H+
?
show the reaction diagram
D-galactose + NADH + H+
? + NAD+
show the reaction diagram
D-galactose + NADPH + H+
?
show the reaction diagram
D-glucose + NADH
?
show the reaction diagram
-
-
-
?
D-glucose + NADH + H+
?
show the reaction diagram
D-glucose + NADPH + H+
?
show the reaction diagram
D-glucose + NADPH + H+
? + NADP+
show the reaction diagram
D-glucosone + NADPH + H+
D-fructose + NADP+
show the reaction diagram
-
catalytic efficiency is 22fold higher than the catalytic efficiency for D-xylose
-
-
?
D-glyceraldehyde + NADH
?
show the reaction diagram
-
-
-
?
D-lyxose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
D-lyxose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-mannose + NADH + H+
?
show the reaction diagram
8% of the activity compared to D-xylose (with NADH as cofactor)
-
-
?
D-ribose + NADH + H+
?
show the reaction diagram
D-ribose + NADPH + H+
?
show the reaction diagram
D-ribose + NADPH + H+
? + NADP+
show the reaction diagram
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
show the reaction diagram
D-xylose + NADH + H+
xylitol + NAD+
show the reaction diagram
D-xylose + NADPH + H+
xylitol + NADP+
show the reaction diagram
DL-glyceraldehyde + NADH + H+
glycerol + NAD+
show the reaction diagram
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
furfural + NADH + H+
(furan-2-yl)methanol + NAD+
show the reaction diagram
L-arabinose + NADH + H+
arabinitol + NAD+
show the reaction diagram
-
low activity in direction of arabinitol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol
-
-
r
L-arabinose + NADH + H+
L-arabinitol + NAD+
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
L-arabinose + NADPH + H+
arabinitol + NADP+
show the reaction diagram
-
low activity in direction of arabinitol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol
-
-
r
L-arabinose + NADPH + H+
L-arabinitol + NADP+
show the reaction diagram
L-arabinose + NADPH + H+
L-arabitol + NADP+
show the reaction diagram
-
-
-
-
?
L-lyxose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
L-lyxose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
methylglyoxal + NADPH + H+
?
show the reaction diagram
-
catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose
-
-
?
pentanal + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
pentanal + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
phenylglyoxal + NADPH + H+
?
show the reaction diagram
-
catalytic efficiency is 17fold higher than the catalytic efficiency for D-xylose
-
-
?
propionaldehyde + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
propionaldehyde + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
pyridine-2-aldehyde + NADPH + H+
?
show the reaction diagram
-
catalytic efficiency is 7fold higher than the catalytic efficiency for D-xylose
-
-
?
valeraldehyde + NADPH + H+
?
show the reaction diagram
-
catalytic efficiency is 13fold higher than the catalytic efficiency for D-xylose
-
-
?
xylitol + NAD+
D-xylose + NADH + H+
show the reaction diagram
xylitol + NADP+
D-xylose + NADPH + H+
show the reaction diagram
xylosone + NADPH + H+
?
show the reaction diagram
-
catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose
-
-
?
xylulose + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
r
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
show the reaction diagram
D-xylose + NADH + H+
xylitol + NAD+
show the reaction diagram
D-xylose + NADPH + H+
xylitol + NADP+
show the reaction diagram
xylitol + NAD+
D-xylose + NADH + H+
show the reaction diagram
xylitol + NADP+
D-xylose + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
NADP+
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
1 mM, stimulates
CoCl2
1 mM, stimulates
FeCl2
1 mM, stimulates
Li+
Ca2+, Li+, Mg2+, Mn2+ and NH4+ at 10 mM decrease activity by 10-50%
Mg2+
Ca2+, Li+, Mg2+, Mn2+ and NH4+ at 10 mM decrease activity by 10-50%
MgCl2
1 mM, stimulates
Mn2+
Ca2+, Li+, Mg2+, Mn2+ and NH4+ at 10 mM decrease activity by 10-50%
MnCl2
1 mM, stimulates
NH4+
Ca2+, Li+, Mg2+, Mn2+ and NH4+ at 10 mM decrease activity by 10-50%
NiCl2
1 mM, stimulates
ZnCl2
1 mM, stimulates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-hydroxymethylfurfural
acetate
mixed inhibition type
acetic acid
-
-
AMP
-
2 mM, completely abolishes D-xylose reduction
ATP
-
2 mM, completely abolishes D-xylose reduction, competitive
cholic acid
-
0.1% (w/v), 30% inhibition
Cu2+
activity is completely restored by addition of EDTA
deoxycholic acid
-
0.1% (w/v), 30% inhibition
dithiothreitol
DTT
1 mM, 35% inhibition
EDTA
-
1 mM, 30% inhibition
furfural
gallic acid
mixed inhibition type
Hg2+
-
0.001 mM, 2 min, complete inhibition
Mn2+
-
25 mM, 95% inhibition
N-bromosuccinimide
-
NADPH protects
NaCl
-
50 mM, 25% inhibition
NADP+
NADPH
-
for monospecific xylose reductase (msXR) and dual specific xylose reductase (dsXR) NADPH behaves as a competitive inhibitor against NADP+. Competitive inhibition of is observed both at unsaturating and saturating concentrations of xylitol
p-chloromercuribenzoate
-
0.001 mM, 2 min, complete inhibition
phenol
competitive inhibition
pyridoxal 5'-phosphate
-
gradual inactivation. NADH, ATP or 2'-AMP protects. No protection by D-xylose
sodium phosphite
-
200 mM, 37% inhibition
Tannic acid
-
-
Vanillin
mixed inhibition type
xylitol
non-competitive against NADH and D-xylose
Zn2+
-
25 mM, 95% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
1 mM, increases activity by 13%
bovine serum albumin
-
cysteine
1 mM, increases activity by 29%
dithiothreitol
1 mM, increases activity by 43%
DTT
1 mM, 27% increase of activity
glutathione
1 mM, increases activity by 21%
Triton X-100
Tween 20
0.1%, the specific activity is increased by 20-30%
Tween 80
0.1%, the specific activity is increased by 20-30%
Tween-20
-
0.1% (w/v), 10-15% activation
Tween-80
-
0.1% (w/v), 10-15% activation
additional information
neither inhibited nor activated by EDTA at concentrations ranging from 1 to 10 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.126 - 0.221
2-deoxy-D-galactose
0.058
2-deoxy-D-glucose
-
pH 7.0, 25C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.038
2-deoxy-D-ribose
-
pH 7.0, 25C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
1.8
benzaldehyde
pH 7.2, temperature not specified in the publication
2 - 33
Butanal
285.4
D-arabinose
pH 6.0
0.02 - 151.7
D-erythrose
0.007 - 0.01
D-fucose
0.015 - 180
D-galactose
0.006 - 360
D-glucose
0.068 - 302
D-ribose
0.01 - 722
D-xylose
1.14 - 2.43
DL-glyceraldehyde
4.2
furfural
pH 7.2, temperature not specified in the publication
0.02 - 93
L-arabinose
0.117 - 0.144
L-Lyxose
0.027 - 0.0587
NAD+
0.0033 - 40
NADH
0.0266
NADP+
-
pH 7, 25C
0.0018 - 7.6
NADPH
3.9 - 14.7
pentanal
13.2 - 78
propionaldehyde
209 - 537
xylitol
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5 - 8.4
2-deoxy-D-galactose
6.8
2-deoxy-D-glucose
-
pH 7.0, 25C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
1.4
2-deoxy-D-ribose
-
pH 7.0, 25C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.027 - 12
9,10-phenanthrenequinone
5.4 - 21.2
Butanal
24.3 - 27.5
D-erythrose
10.2 - 20.7
D-fucose
9.4 - 1800
D-galactose
8.2 - 1320
D-glucose
4.9 - 3120
D-ribose
0.002 - 324000
D-xylose
14.1 - 24.3
DL-glyceraldehyde
13.5 - 1800
L-arabinose
5.6
L-idose
-
pH 7.0, 25C, dual specific xylose reductase, cofactor: NADH
6.6 - 18.4
L-Lyxose
0.89 - 0.92
NAD+
4.7 - 25110
NADH
0.82
NADP+
-
pH 7, 25C
2.6 - 324000
NADPH
5.9 - 20.7
pentanal
4.6 - 6.9
propionaldehyde
0.87 - 0.92
xylitol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.7 - 38
2-deoxy-D-galactose
117
2-deoxy-D-glucose
-
pH 7.0, 25C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
36.8
2-deoxy-D-ribose
-
pH 7.0, 25C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
20 - 2300
9,10-phenanthrenequinone
0.16 - 0.93
Butanal
0.028
D-arabinose
pH 6.0
0.089 - 1380
D-erythrose
1457 - 2070
D-fucose
0.16 - 627
D-galactose
0.05 - 1370
D-glucose
0.043 - 134
D-ribose
0.0009 - 27430
D-xylose
0.3 - 21.3
DL-glyceraldehyde
0.75 - 1230
L-arabinose
46 - 157
L-Lyxose
15.2 - 34.1
NAD+
81.7 - 83750
NADH
30.9
NADP+
-
pH 7, 25C
6.2 - 1466000
NADPH
0.4 - 5.31
pentanal
0.035 - 0.09
propionaldehyde
0.0034 - 0.031
xylitol
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
45
5-hydroxymethylfurfural
pH 7.0, 45C
100
acetate
pH 7.0, 45C
0.0239
ATP
-
pH 7, 25C, variable substrate: NADH
0.034
Cu2+
pH 6.0
54
furfural
pH 7.0, 45C
32
gallic acid
pH 7.0, 45C
0.074 - 0.65
NAD+
0.0019 - 0.02
NADH
0.0015 - 0.17
NADP+
0.014
NADPH
-
pH 7.0, 25C, dual specific xylose reductase (dsXR)
11
phenol
pH 7.0, 45C
0.1
Vanillin
pH 7.0, 45C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
5-hydroxymethylfurfural
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.021
-
crude enzyme extract, induced cells, pH 6.0, 40C
0.027
-
crude enzyme extract, induced cells, pH 6.0, 70C
0.11
Torulopsis molishiama
-
-
0.16 - 0.4
-
recombinant enzyme in transgenic strains of Saccharomyces cerevisiae
0.48
-
cell extract
1.11 - 2.52
recombinant strains harboring genes xyl1 and mutated XDH, pH and temperature not specified in the publication, substrates D-xylosse and NADPH
1.39 - 1.56
-
NADH-dependent activity
2
-
mutant enzyme Y49F
2.4
mutant K21A, substrate NADH, pH 6.5, 35C
2.86
-
recombinant strain LNG2, pH 7.0, 25C, xylose reduction with NADPH
3.4
-
NADPH-dependent activity
4.84
-
NADPH-dependent activity
4.93
-
NADH-dependent activity
5
mutant K21A, substrate NADPH, pH 6.5, 35C
6.6
wild-type, substrate NADH, pH 6.5, 35C
10.37
-
NADH-dependent activity
11.16
-
pH 7.0, 25C
16.7
-
NADH-dependent activity
20.3
wild-type, substrate NADPH, pH 6.5, 35C
22.1
-
NADPH-dependent activity
23.2
-
NADPH-dependent activity
47.8
-
D-xylose reductase 3
56.9
-
D-xylose reductase 1
81
-
D-xylose reductase 2
104
-
wild-type enzyme
251.5
cofactor: NADPH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
assay at
8.9
-
xylitol oxidation
additional information
-
use of response surface analysis for the maximization of xylose reductase activity as a function of pH and temperature. This methodology also makes it possible to determine a desirable working region where a high xylose reductase to xylitol dehydrogenase ratio can be attained