Information on EC 1.1.1.307 - D-xylose reductase

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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
Metabolic pathways
-
-
Pentose and glucuronate interconversions
-
-
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
strain F-3
-
-
Manually annotated by BRENDA team
strain F-3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
KFCC-10875
SwissProt
Manually annotated by BRENDA team
strain VGI-II
-
-
Manually annotated by BRENDA team
strain VGI-II
-
-
Manually annotated by BRENDA team
Candida tenuis CBS 4435
strain CBS 4435
SwissProt
Manually annotated by BRENDA team
Candida tropicalis ATCC 20336
-
-
-
Manually annotated by BRENDA team
IF0 0618
-
-
Manually annotated by BRENDA team
Candida tropicalis SCTCC 300249
SCTCC 300249
UniProt
Manually annotated by BRENDA team
strain Y-456
-
-
Manually annotated by BRENDA team
gene XYL1
-
-
Manually annotated by BRENDA team
gene XYL1
-
-
Manually annotated by BRENDA team
strain UFV-170 XR
-
-
Manually annotated by BRENDA team
strain UFV-170 XR
-
-
Manually annotated by BRENDA team
Y-488
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
FTI 20037
-
-
Manually annotated by BRENDA team
strain Y-1017
-
-
Manually annotated by BRENDA team
strain Y-1532, strain Y-1533, strain Y-1634
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Y-1632
-
-
Manually annotated by BRENDA team
strain Y-2160
-
-
Manually annotated by BRENDA team
Torulopsis molishiama
strain 55
-
-
Manually annotated by BRENDA team
Torulopsis molishiama 55
strain 55
-
-
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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 + 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-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-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
additional information
-
Kluyveromyces marxianus strains expressing Pichia stipitis Psxyl1 genes show reversed cofactor specificity, overview
-
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
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
Hg2+
-
0.001 mM, 2 min, complete inhibition
Mn2+
-
25 mM, 95% inhibition
N-bromosuccinimide
-
NADPH protects
NaCl
-
50 mM, 25% inhibition
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
pyridoxal 5'-phosphate
-
gradual inactivation. NADH, ATP or 2'-AMP protects. No protection by D-xylose
sodium phosphite
-
200 mM, 37% inhibition
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
Candida intermedia
-
pH 7.0, 25C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
1.4
2-deoxy-D-ribose
Candida intermedia
-
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
Candida intermedia
-
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+
Candida tenuis
-
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
Candida intermedia
-
pH 7.0, 25C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
531
36.8
2-deoxy-D-ribose
Candida intermedia
-
pH 7.0, 25C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
2811
20 - 2300
9,10-phenanthrenequinone
0.16 - 0.93
Butanal
0.028
D-arabinose
Candida parapsilosis
Q6Y0Z3
pH 6.0
565
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+
Candida tenuis
-
pH 7, 25C
10
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
0.0239
ATP
-
pH 7, 25C, variable substrate: NADH
0.034
Cu2+
pH 6.0
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)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.11
Torulopsis molishiama
-
-
0.16 - 0.4
-
recombinant enzyme in transgenic strains of Saccharomyces cerevisiae
0.48
-
cell extract
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
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6.5
pH 4.0: about 55% of maximal activity, pH 6.5: about 60% of maximal activity
4 - 7
-
pH 4.0: about 40% of maximal activity, pH 7.0: about 50% of maximal activity
4.5 - 7.5
-
pH 4.5: about 55% of maximal activity, pH 7.5: about 50% of maximal activity
5 - 7
pH 5.0: 81% of maximal activity, pH 7.0: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 40
-
activity increases linearly from 25C to 50C
25 - 65
-
25C: about 55% of maximal activity, 65C: about 65% of maximal activity
30 - 60
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.1
-
D-xylose reductase 2, isoelectric focusing, pH-range: 2.5-5.0
4.15
-
D-xylose reductase 1, isoelectric focusing, pH-range: 2.5-5.0
4.7
-
isoelectric focusing
5.19
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
the organism grows on rice straw hemicellulosic hydrolysate, as the only source of nutrient, optimization of culture conditions for production of xylitol from D-xylose, xylitol dehydrogenase remains constant, whereas the level of xylose reductase decreases when the initial xylose concentration is increased from 30 to 70 g/l, development of enzyme activities, overview
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
gel filtration
53000
-
gel filtration
58000
-
D-xylose reductase 1, D-xylose reductase 2, D-xylose reductase 3, gel filtration
60000
-
gel filtration
63000 - 65000
-
gel filtration
69000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 43000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the purified N309D mutant is crystallized by the hanging-drop vapour-diffusion method at 25C. The best-diffracting crystals are grown using a well solution consisting of 2.1 M (NH4)2SO4, 100 mM sodium acetate and 100 mM sodium citrate, pH 6.4. 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
-
hanging-drop vapour diffusion method, to 2.91 A resolution. Unit cell belongs to space group P31 or P32, presence of four XR molecules in the asymmetric unit, with 68.0% solvent content; hanging-drop vapour-diffusion method. X-ray diffraction data from xylose reductase crystals at 2.91 A resolution, the unit cell belongs to space group P3(1) or P3(2). Preliminary analysis indicates the presence of four xylose reductase molecules in the asymmetric unit, with 68.0% solvent content
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
below pH 5 and above pH 8.0 the enzyme is inactivated within 3-6 days
286260
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
60 days, 50% loss of activity
20
8 days, 50% loss of activity
21
-
at room temperature stable for more than 1 month
25
-
half-life: more than 2 months
30
3 days, 50% loss of activity
30 - 35
-
48 h, stability starts to decrease above 30-35C
40
-
half-life: 94 min
45
4.5 h, 50% loss of activity
50
2 min, 50% loss of activity
additional information
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non-ionic detergents and bovine serum albumin stabilize the enzyme to a significant extent during long-term incubation at 25C, 30C or 38C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable enzyme at 25C in phosphate and Tris buffer of various ionic strengths between pH 6.0 and 7.0
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme undergoes thiol oxidation during storage or purification
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286260
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, 4 months, activity in cell extract remains stable
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-20C, pure enzyme preparation is stable for more than 4 months
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38C, 3 h, activity in cell extract remains stable
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4C, 3 h, activity in cell extract remains stable
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4C, enzyme retains activity for several months
4C, pure enzyme preparation is stable for more than 4 months
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4C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant enzyme
; recombinant protein
identification of the most suitable operating conditions for purification, the aqueous two-phase systems proves effective for partial purification of xylose reductase in cell-free crude extract
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recombinant enzyme
recombinant His-tagged enzyme from Escherichia coli strain UT5600 by nickel affinity chromatography
wild-type and mutant enzyme Y49F
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of Kluyveromyces marxianus strains expressing Pichia stipitis Psxyl1 genes leading to reversed cofactor specificity and ethanol and xylitol production
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expressed in Escherichia coli BL21 (DE3), subloned into the pYES2 vector and transformed into Saccharomyces cerevisiae W303-1A
expression in Candida tropicalis increases production of ethanol and glycerol
expression in Escherichia coli
expression in Escherichia coli as a His6-tagged fusion protein
expression in Escherichia coli as a His6-tagged fusion protein in high yield
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expression in Escherichia coli; expression of histidine-tagged wild type Texr and mutant Texr K271R/N273D in Escherichia coli BL21-Star DE3
expression in Escherichia coli; subcloned into the expression plasmid pET28a(+) and subsequently transformed into Escherichia coli BL21(DE3)pLysS cells for recombinant protein expression
expression of His-tagged enzyme in Escherichia coli
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expression of single-site mutant xylose reductase from Candida tenuis (CtXR (K274R)) results in recombinant Corynebacterium glutamicum strain CtXR4 that produces 26.5 g/l xylitol at 3.1 g/l*h. To eliminate possible formation of toxic intracellular xylitol phosphate, genes encoding xylulokinase (XylB) and phosphoenolpyruvate-dependent fructose phosphotransferase (PTSfru) are disrupted to yield strain CtXR7
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expression of the mutant xylulose reductase from Candida tenuis in Saccharomyces cerevisiae, co-expression with an engineered xylitol dehydrogenase, with altered cofactor specificity, from Galactocandida mastotermitis, the transformed strain shows up to 50% decreased glycerol yield without increase in ethanol during xylose fermentation, overview
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gene XYL1
gene ZMO0976, expression of His-tagged enzyme in Escherichia coli strain UT5600
overexpression of wild-type enzyme and mutant enzyme, with modified cofactor specificity, in Saccharomyces cerevisiae strain CEN.PK 113-7D under control of the constitutive TDH3 promoter, coexpression with xylitol dehydrogenase from Galactocandida mastotermitis, The strain harboring the xylose reductase double mutant shows 42% enhanced ethanol yield compared to the reference strain harboring wild-type xylose reductase during anaerobic bioreactor conversions of xylose. Likewise, the yields of xylitol and glycerol are decreased by 52% and 57% respectively in the xylose reductase mutant strain
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the cofactor preference of Pichia stipitis xylose reductase is altered by site-directed mutagenesis. When the K270R xylose reductase is combined with a metabolic engineering strategy that ensures high xylose utilization capabilities, a recombinant Saccharomyces cerevisiae strain is created that provides a unique combination of high xylose consumption rate, high ethanol yield and low xylitol yield during ethanolic xylose fermentation
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
formation of xylose reductase in the yeast Candida tropicalis is significantly repressed in cells grown on medium that contains glucose as carbon and energy source, because of the repressive effect of glucose
the Aspergillus niger transcriptional activator XlnR, which is involved in the degradation of the polysaccharides xylan and cellulose, also regulates D-xylose reductase gene expression
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D50A
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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
H113A
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mutation causes a 10000-100000fold decrease in the rate constant for hydride transfer from NADH to 9,10-phenanthrenequinone, whose value in the wild-type enzyme is about 800 per s
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
L80A
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mutation causes a 10000-100000fold decrease in the rate constant for hydride transfer from NADH to 9,10-phenanthrenequinone, whose value in the wild-type enzyme is about 800 per s
N309A
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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