Information on EC 1.1.1.10 - L-xylulose reductase

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

EC NUMBER
COMMENTARY hide
1.1.1.10
-
RECOMMENDED NAME
GeneOntology No.
L-xylulose reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xylitol + NADP+ = L-xylulose + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-glucuronate degradation I
-
-
L-arabinose degradation II
-
-
Metabolic pathways
-
-
Pentose and glucuronate interconversions
-
-
SYSTEMATIC NAME
IUBMB Comments
xylitol:NADP+ 4-oxidoreductase (L-xylulose-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-17-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fragment; yeast, strain NRRL Y-1484
SwissProt
Manually annotated by BRENDA team
gene dhs-21
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 4D2P
-
-
Manually annotated by BRENDA team
strain 4D2P
-
-
Manually annotated by BRENDA team
strain FTI
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
xylitol utilizing mutant strains, e.g. DM101, of strain 19321
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene lxr3 or tre60033
UniProt
Manually annotated by BRENDA team
gene lxr3 or tre60033
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-dibromo-2,3-butanedione + NAD(P)H
? + NAD(P)+
show the reaction diagram
1,4-dibromo-2,3-butanedione + NADPH
? + NADP+
show the reaction diagram
-
dicarbonyl reductase activity
-
-
r
D-erythrose + NADPH
?
show the reaction diagram
D-erythrose + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
ir
D-fructose + NADPH + H+
? + NADP+
show the reaction diagram
low activity
-
-
?
D-ribulose + NADH
D-arabinitol + NAD+
show the reaction diagram
-
-
-
r
D-ribulose + NADPH
D-ribitol + NADP+
show the reaction diagram
D-ribulose + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
D-ribulose + NADPH + H+
D-ribitol + NADP+
show the reaction diagram
-
-
-
-
?
D-sorbitol + NADP+
?
show the reaction diagram
-
-
-
-
?
D-sorbitol + NADP+
D-sorbose + NADPH + H+
show the reaction diagram
D-threose + NADPH
D-threitol + NADP+
show the reaction diagram
D-threose + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
ir
D-xylulose + NADH + H+
D-arabinitol + NAD+
show the reaction diagram
D-xylulose + NADPH + H+
D-xylitol + NADP+
show the reaction diagram
D-xylulose + NADPH + H+
xylitol + NADP+
show the reaction diagram
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
diacetyl + NADPH + H+
acetoin + NADP+
show the reaction diagram
-
-
-
-
?
DL-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
show the reaction diagram
DL-threitol + NAD+
D-threose + NADH
show the reaction diagram
DL-threitol + NADP+
D-erythrulose + NADPH
show the reaction diagram
-
probably identical with erythrulose reductase, EC 1.1.1.162 and diacetyl reductase, EC 1.1.1.5
-
r
L-erythrulose + NADPH
?
show the reaction diagram
L-erythrulose + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
ir
L-ribulose + NADPH + H+
? + NADP+
show the reaction diagram
low activity
-
-
?
L-sorbose + NADPH + H+
L-sorbitol + NADP+
show the reaction diagram
L-threose + NADPH
L-threitol + NADP+
show the reaction diagram
L-xylulose + NADH
L-xylitol + NAD+
show the reaction diagram
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
L-xylulose + NADPH + H+
xylitol + NADP+
show the reaction diagram
xylitol + NADP+
L-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
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
-
detoxification of alpha-dicarbonyl compounds
-
-
r
L-xylulose + NADH
L-xylitol + NAD+
show the reaction diagram
Q70FD1
part of the L-arabinose catabolism
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
L-xylulose + NADPH + H+
xylitol + NADP+
show the reaction diagram
Q21929
-
-
-
ir
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
additional information
?
-
Q21929
dicarbonyl/L-xylulose reductase is bifunctional
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-hydroxybutyric acid
4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide
4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide
-
IC50: 0.0003 mM for wild-type enzyme, 0.00056 mM for mutant enzyme L143F, 0.002 mM for mutant enzyme H146L, 0.0002 mM for mutant enzyme W191S, 0.0022 mM for mutant enzyme W191F
acetoacetic acid
aminopyrine
-
70 mM
cysteine
-
the addition of cysteine (more than 2 mM) inactivates human L-xylulose reductase and is accompanied by a 10fold decrease in catalytic efficiency, the activity of the cysteine-inactivated enzyme is not recovered by the addition of 10 mM dithiothreitol and 2-mercaptoethanol
fluoride
-
50 mM
heptanoic acid
hexanoic acid
iodoacetate
n-butyric acid
Octanoic acid
50% inhibition at 2.5 mM
oxaloacetic acid
p-chloromercuribenzoate
-
-
pentanoic acid
Phosphate buffer
-
-
-
potassium phosphate
-
when the purified enzyme containing 2 mM 2-mercaptoethanol is diluted with 10 mM potassium phosphate pH 7.0, its diacetyl reductase activity is gradually decreased
Propionic acid
Pyruvic acid
threonic acid
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 0.139
1,4-dibromo-2,3-butanedione
1.5 - 13
acetoin
2.7
D-arabinitol
pH 9.0, 30C, purified recombinant enzyme
0.27 - 6
D-erythrose
4.7 - 150
D-ribulose
250
D-sorbitol
pH 7.0, 30C, recombinant enzyme
14 - 37
D-threitol
0.68 - 4
D-threose
2.58 - 18
D-xylulose
0.077 - 42
diacetyl
1.6 - 60
dihydroxyacetone
1.2 - 6
DL-glyceraldehyde
0.17 - 5.5
L-erythrulose
0.18
L-ribulose
pH 7.0, temperature not specified in the publication
2.9 - 8.3
L-threose
0.0099 - 7.2
L-xylitol
0.05 - 25
L-xylulose
0.85 - 1.5
NAD+
0.12 - 0.69
NADH
0.00067 - 0.153
NADP+
0.002 - 97
NADPH
10 - 1239
xylitol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65 - 6.9
acetoin
0.43 - 23
D-erythrose
0.52 - 119
D-ribulose
1.8
D-sorbitol
Trichoderma reesei
G0RH19
pH 7.0, 30C, recombinant enzyme
0.48 - 16
D-threitol
0.82 - 32
D-threose
0.1 - 19
D-xylulose
0.0008 - 41
diacetyl
0.23 - 8.7
dihydroxyacetone
0.52 - 24
DL-glyceraldehyde
0.6 - 25
L-erythrulose
0.49
L-ribulose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
0.52 - 27
L-threose
0.65 - 39
L-xylulose
1.5 - 55
NAD+
2 - 76
NADH
0.65 - 26
NADP+
0.0005 - 34
NADPH
0.6 - 20
xylitol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.75
D-erythrose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
1442
3.42
D-threose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
2881
0.47
D-xylulose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
715
19.03
L-erythrulose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
1981
0.36
L-ribulose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
1621
7.55
L-xylulose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
1238
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00037 - 0.00044
4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00023
4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide
Rattus norvegicus
-
IC50: 0.00023 mM for wild-type enzyme, 0.0019 mM for mutant enzyme L143F, 0.0018 mM for mutant enzyme H146L, 0.0029 mM for mutant enzyme W191S, 0.00079 mM for mutant enzyme W191F
0.0003
4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide
Rattus norvegicus
-
IC50: 0.0003 mM for wild-type enzyme, 0.00056 mM for mutant enzyme L143F, 0.002 mM for mutant enzyme H146L, 0.0002 mM for mutant enzyme W191S, 0.0022 mM for mutant enzyme W191F
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.23 - 0.32
-
xylitol dehydrogenase activity
1
-
substrate xylitol, pH 7.0, 22C
1.4
-
substrate ribulose, pH 7.0, 22C
1.8
-
substrate L-xylulose, pH 7.0, 22C
33
-
xylitol oxidation, NADP+
143
purified native enzyme, L-xylulose reductase activity
200
-
L-xylulose reduction, NADPH
642
purified native enzyme, L-xylulose reductase activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
reduction of L-xylulose
7.5
-
approximately
10 - 11
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oxidation of xylitol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.5
-
pH 4.5: about 55% of maximal activity, pH 8.5: about 70% of maximal activity, reductase activity
5 - 8.5
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reduction of L-xylulose
7 - 10.5
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pH 7.0: about 40% of maximal activity, pH 10.5: about 60% of maximal activity, oxidase activity
8 - 11.5
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oxidation of xylitol
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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reductase activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 55
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15C: about 65% of maximal activity, 55C: about 60% of maximal activity, reductase activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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epididymal
Manually annotated by BRENDA team
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expression levels of L-xylulose reductase and its mRNA in the T lymphoma cells are markedly enhanced after the exposure to 9,10-phenanthrenequinone, and the induction is completely abolished by the ROS scavengers. L-Xylulose reductase is upregulated in the earlier step of the apoptosis and deteriorates the apoptotic signaling through the generation of ROS by the redox cycling of 9,10-phenanthrenequinone
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
102000
-
4D2P, nondenaturing PAGE
136000
-
non-denaturing PAGE
250000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
x-ray crystallography
octamer
-
8 * 32000, SDS-PAGE
tetramer
additional information
-
the dimeric form is inactive
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
18 mg/ml purified enzyme complexed with NADPH, in 10 mM Tris-HCl, pH 7.5, 2 mM 2-mercaptoethanol, 20% glycerol, replacement buffer is 10 mM Tris-HCl, pH 7.5, 2 mM 2-mercaptoethanol, mixed with 12.9 mM NADPH, in a molar ratio of enzyme and cofactor of 1:8, equal volume of 0.003 ml of enzyme complex mixture and well solution, containing 15% PEG 8000, 50 mM potassium phosphate, and 0.1 M MES, pH 6.5, 1 week, X-ray diffraction structure determination and analysis, molecular replacement method, 1.96 A resolution, molecular modeling
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crystal structure analysis and modelling
-
structure of the biological tetramer of human L-xylulose reductase in complex with NADP+ and the competitive inhibitor 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide, vapor diffusion method
-
vapour diffusion method, using 15% PEG 8000, 0.05 M potassium phosphate and 0.1 M MES buffer, pH 6.5
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
2C, 2 h stable
285663
9
-
room temperature, several h stable
285663
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
20 min stable
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation during dialysis
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, mitochondria, 0.15 M KCl- 0.01 M NaHCO3, minimum 2 days
-
2C, aqueous solution, many weeks
-
4C, Tris-HCl 20 mM, pH 7.0, at leat several weeks
-
frozen, ammonium sulfate precipitate, several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial from strain DM101
-
recombinant enzyme
-
recombinant enzyme from Escherichia coli, native from liver
recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
recombinant N-terminal His-tagged enzyme from Saccharomyces cerevisiae strain CEN.PK2-1D by nickel affinity chromatography
recombinant wild-type and mutant enzymes from Escherichia coli
-
strain 4D2P, partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a recombinant Saccharomyces cerevisiae strain D-XR/ARSdR/XK, in which protein engineered NADP+-dependent XDH is expressed, shows 40% increased ethanol production and 23% decrease in xylitol excretion as compared with the reference strain D-XR/XDH/XK expressing the wild-type XDH
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construction of a cDNA library, DNA sequence determination and analysis, subcloning in Escherichia coli DH5alpha, overexpression as His-tagged enzyme in Saccharomyces cerevisiae strain CEN.PK2
DNA sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli as a His6 tag fusion protein
-
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae strain MA-R4
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expressed in Saccharomyces cerevisiae strains MA-N2, MA-N3, MA-N4, and MA-N5
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expression in Saccharomyces cerevisiae
-
expression of Pichia stipitis mutated XYL2 (D207/I208R/F209S or XYL2 S96C/S99C/Y102C/D207A/I208R/F209S) in Saccharomyces cerevisiae
-
expression of wild-type and mutant enzymes in Escherichia coli
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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gene dhs-21, DNA and amino acid sequence determination and analysis, the dhs-21 gene is physically mapped to the cosmid R11D1 between the sma-1 and mes-4genes on chromosome V, expression of His6-tagged enzyme. Spatial and temporal expression pattern of the DHS-21-GFP construct in transgenic worms, overview
gene lxr3, phylogenetic analysis, cloning in Escherichia coli strain JM109, expression of N-terminal His-tagged in Saccharomyces cerevisiae strain CEN.PK2-1D
Tn5 transposon transfer
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transgenic mice over-expressing dicarbonyl/L-xylulose reductase gene crossed with KK-A(y) diabetic model mice serve as an animal model for the metabolism of renal carbonyl compounds
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is upregulated upon growth on L-arabinose
-
knock-down of daf-16 and elt-2 transcription factors affects dhs-21 expression
transcription of lxr3 is specifically induced by L-arabinose and L-arabitol
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N107D
-
site-directed mutagenesis, active site residue mutant, inactive
N107L
-
site-directed mutagenesis, active site residue mutant, inactive
D238E
-
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
D238E/L242W
-
site-directed mutagenesis, mutation leads to complete prevention of cold inactivation, mutant exists in tetrameric form at low temperature
D238E/L242W/T244C
-
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
L242W
-
site-directed mutagenesis, mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
L242W/T244C
-
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
T244C
-
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
K153M
-
site-directed mutagenesis, active site mutant, complete loss of activity
N190V
-
site-directed mutagenesis, altered activity
N190V/W191S
-
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity
N190V/W191S/Q137M/L143F/H146L
-
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows high 3-ketosteroid reductase activity
Q137M
-
site-directed mutagenesis, altered activity, stable against cold inactivation
Q137M/F241L
-
site-directed mutagenesis, altered activity, sensitive to cold inactivation like the wild-type enzyme
Q137M/L143F
-
site-directed mutagenesis, increased Km for L-xylulose compared to the wild-type
Q137M/L143F/H146L
-
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows 3-ketosteroid reductase activity
S136A
-
site-directed mutagenesis, active site mutant, complete loss of activity
Y149F
-
site-directed mutagenesis, active site mutant, complete loss of activity
D207/I208R/F209S
-
kcat/Km of mutant enzyme for NAD+ dropps 15fold compared with the native enzyme, kcat/Km for NADP+ increases up to 4100fold
S96C/S99C/Y102C/D207A/I208R/F209S
-
mutation produces a further 4fold improvement in the kcat/Km for NADP+ compared to mutant enzyme D207/I208R/F209S
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
-
enzyme is a target for design and development of potent and specific structure-based inhibitors binding in the active site