Information on EC 1.1.1.9 - D-xylulose reductase

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

EC NUMBER
COMMENTARY hide
1.1.1.9
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RECOMMENDED NAME
GeneOntology No.
D-xylulose reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xylitol + NAD+ = D-xylulose + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
xylitol degradation
-
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degradation of sugar alcohols
-
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Pentose and glucuronate interconversions
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming)
Also acts as an L-erythrulose reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-16-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a DELTApyrG strain developed from strain KBN616
SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
CBS 4435
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Manually annotated by BRENDA team
CBS 4435
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain CFN42
UniProt
Manually annotated by BRENDA team
formerly Pichia stipitis
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
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
D-arabitol + NAD+
?
show the reaction diagram
-
-
-
-
?
D-arabitol + NAD+
? + NADH + H+
show the reaction diagram
D-fructose + NADH + H+
D-sorbitol + NAD+
show the reaction diagram
D-fructose + NADH + H+
sorbitol + NAD+
show the reaction diagram
D-iditol + NAD+
?
show the reaction diagram
D-mannitol + NAD+
?
show the reaction diagram
D-mannitol + NAD+
? + NADH + H+
show the reaction diagram
8% of the activity with xylitol
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
D-ribulose + NADH
D-ribitol + NAD+
show the reaction diagram
-
-
-
r
D-ribulose + NADH + H+
?
show the reaction diagram
-
-
-
?
D-sorbitol + NAD+
? + NADH + H+
show the reaction diagram
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-sorbitol + NAD+
L-sorbose + NADH + H+
show the reaction diagram
D-threitol + NAD+
?
show the reaction diagram
D-xylitol + NAD+
D-xylulose + NADH
show the reaction diagram
D-xylulose + NAD+
xylitol + NADH + H+
show the reaction diagram
-
-
-
-
r
D-xylulose + NADH + H+
D-xylitol + NAD+
show the reaction diagram
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
dihydroxyacetone + NADH
glycerol + NAD+
show the reaction diagram
-
-
-
-
-
erythritol + NAD+
? + NADH + H+
show the reaction diagram
0.77% of the activity with xylitol
-
-
?
erythritol + NAD+
L-erythrulose + NADH
show the reaction diagram
-
-
-
r
galactitol + NAD+
? + NADH + H+
show the reaction diagram
0.98% of the activity with xylitol
-
-
?
glycerol + NAD+
?
show the reaction diagram
L-arabinitol + NAD+
? + NADH + H+
show the reaction diagram
21% of the activity with xylitol
-
-
?
L-arabitol + NAD+
?
show the reaction diagram
L-arabitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
L-erythrulose + NADH
erythritol + NAD+
show the reaction diagram
L-iditol + NAD+
?
show the reaction diagram
-
-
-
-
?
L-sorbose + NADH + H+
?
show the reaction diagram
-
-
-
?
L-threitol + NAD+
? + NADH + H+
show the reaction diagram
L-xylulose + NADH
L-xylitol + NAD+
show the reaction diagram
-
-
-
-
?
meso-erythritol + NAD+
? + NADH + H+
show the reaction diagram
ribitol + NAD+
?
show the reaction diagram
ribitol + NAD+
? + NADH + H+
show the reaction diagram
40% of the activity with xylitol
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
Xylitol + NAD+
?
show the reaction diagram
xylitol + NAD+
D-xylose + NADH + H+
show the reaction diagram
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
xylitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
xylitol + NADP+
D-xylulose + NADPH + H+
show the reaction diagram
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-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
Xylitol + NAD+
?
show the reaction diagram
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
1 mM, 18% of the activity with Mg2+
Co2+
1 mM, 38% of the activity with Mg2+
Cu2+
1 mM, 51% of the activity with Mg2+
KCl
-
slight activation
MnCl2
-
10 mM, increase of activity by 100%
NaCl
-
activation
NH4Cl
-
activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
9.2% residual activity at 1 mM
AgNO3
Ca2+
-
complete inhibition at 1 mM
CaCl2
Cd2+
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complete inhibition at 1 mM
CdCl2
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complete inhibition
Co2+
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6.8% residual activity at 1 mM
CuCl2
-
strong inhibition
CuSO4
cysteine
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at 294 mM
D-xylulose
Fe3+
-
18% residual activity at 1 mM
furfural
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weak inhibition
HgCl2
iodoacetamide
-
complete inhibition
iodoacetate
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complete inhibition
iodoacetic acid
K4[Fe(CN)6]
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weak inhibition
Mg2+
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complete inhibition at 1 mM
MgCl2
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10 mM, 4% inhibition
MgSO4
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complete inhibition at 1 mM
Mn2+
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8.4% residual activity at 1 mM
N-ethylmaleimide
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complete inhibition
Na+
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complete inhibition at 1 mM
NaCl
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at 160 mM
NADH
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product inhibition
NH4Cl
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at 310 mM
Ni2+
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11.3% residual activity at 1 mM
NiCl2
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1 mM, complete inhibition
o-phenanthroline
p-chloromercuribenzoic acid
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complete inhibition
Pb(CH3COO)2
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-
Pb2+
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complete inhibition at 1 mM
PCMB
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complete inhibition
phenylmethanesulfonyl fluoride
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weak inhibition
Tiron
A0A1B4XTS0
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trypsin inhibitor T-9378
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weak inhibition
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trypsin-chymotrypsin inhibitor T-9777
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weak inhibition
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ZnSO4
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
D-glucose
-
induces activity
D-Lyxose
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induces activity
D-xylose
glycerol
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induces activity
glycine
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slight activation
GSH
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activation
L-arabinose
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induces activity
Sodium acetate
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1 g/l in reaction medium, about 15% increase of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.8
D-fructose
-
at pH 7.0 and 30C
0.7
D-ribulose
35C, pH 7.5, native enzyme
4 - 31.5
D-sorbitol
12 - 94
D-xylitol
0.66 - 43.9
D-xylulose
31.1
L-arabitol
A0A1B4XTS0
at pH 7.0 and 30C
0.9
L-sorbose
35C, pH 7.5, native enzyme
0.027 - 500
NAD+
0.037 - 36.4
NADH
0.0205 - 170
NADP+
15.8 - 496
ribitol
0.16 - 785
sorbitol
0.039 - 175.5
xylitol
13.8
xylulose
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
920
D-fructose
-
25C, pH 7.5, Tris-HCl
74
D-ribulose
35C, pH 7.5, native enzyme
8.28 - 528
D-sorbitol
302.9 - 1800
D-xylulose
3.35
L-arabitol
A0A1B4XTS0
at pH 7.0 and 30C
216
L-sorbose
35C, pH 7.5, native enzyme
0.052 - 30.33
NAD+
0.017 - 210
NADP+
4.5
ribitol
A0A1B4XTS0
at pH 7.0 and 30C
1.19 - 161
sorbitol
1.12 - 2644
xylitol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.39
D-sorbitol
A0A1B4XTS0
at pH 7.0 and 30C
0.11
L-arabitol
A0A1B4XTS0
at pH 7.0 and 30C
0.03 - 32.37
NAD+
0.018 - 0.56
NADP+
0.29
ribitol
A0A1B4XTS0
at pH 7.0 and 30C
1.12 - 23.7
xylitol
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
D-xylulose
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005
ZnSO4
Candida sp. HA 167
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value identical for wildtype and for mutant E154C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.08
A0A1B4XTS0
crude enzyme, at pH 7.0 and 30C
0.15 - 0.18
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depending on nitrogen source in culture medium
0.76
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purified native enzyme, pH 11.0, 30C, substrate meso-erythritol
2.1
purified native enzyme, substrate xylitol, pH 7.0, 30C
2.16
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specific activity of recombinant Saccharomyces cerevisiae strain TMB3057
4.9
A0A1B4XTS0
after purification, at pH 7.0 and 30C
6.74
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purified native enzyme, pH 11.0, 30C, substrate D-arabitol
11.7
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purified recombinant wild-type enzyme, pH 9.0, 35C
12.89
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purified native enzyme, pH 11.0, 30C, substrate D-mannitol
14.2
purified recombinant His6-tagged enzyme, substrate D-mannitol, pH 11.0, 30C; purified recombinant His6-tagged enzyme, substrate xylitol, pH 7.0, 30C
57.8
-
purified native enzyme, pH 9.0, 35C
87.8
purified recombinant His6-tagged enzyme, substrate xylitol, pH 11.0, 30C
102.5
-
purified native enzyme, pH 11.0, 30C, substrate xylitol
113
-
substrate D-xylitol, pH 10, 30C
135.2
purified recombinant His6-tagged enzyme, substrate D-sorbitol, pH 11.0, 30C
151.4
purified recombinant His6-tagged enzyme, substrate D-fructose, pH 11.0, 30C
156.1
-
purified native enzyme, pH 11.0, 30C, substrate D-sorbitol
180.4
-
purified native enzyme, pH 5.0, 30C, substrate D-fructose
220
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substrate D-sorbitol, pH 10, 30C
250
-
pH 8.4, 30C
326.3
purified recombinant His6-tagged enzyme, substrate D-xylulose, pH 11.0, 30C
564
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purified native enzyme, pH 5.0, 30C, substrate D-xylulose
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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reduction reaction
6.7
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reduction of erythrulose
7.2
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xylitol formation
9.1 - 10
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substrate oxidation, plateau
10.5 - 11
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oxidation reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11
4.5 - 10.5
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activity range, profile overview
8.7 - 10.5
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about 80% of maximal oxidation activity at pH 8.7 and 10.5
9 - 10
-
fully active
9 - 12
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oxidation reaction, activity range
10 - 12
over 60% of maximal activity within this range for reduction of D-xylulose, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 55
A0A1B4XTS0
activity range, inactive at 60C
10 - 65
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activity range, inactivation above
20 - 50
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20C: about 50% of maximal activity, 50C: about 50% of maximal activity
20 - 55
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activity range, profile overview
25 - 40
35 - 68
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about half-maximal activity at 35C and 68C
45 - 55
A0A1B4XTS0
the enzyme partially loses its activity at 45-55C and also completely loses activity at temperatures greater than 60C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
-
isoelectric focusing
6
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT