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Information on EC 1.1.1.10 - L-xylulose reductase and Organism(s) Rattus norvegicus and UniProt Accession Q920P0

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.10 L-xylulose reductase
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q920P0 not found.
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
hide
xylitol
+
NADP+
=
L-xylulose
+
NADPH
+
H+
+
=
+
+
Synonyms
xylose reductase, l-xylulose reductase, dicarbonyl/l-xylulose reductase, nad(p)h-dependent xylose reductase, rplxr, nadp(+)-dependent xylitol dehydrogenase, rplxr3, nadp+-dependent xylitol dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
reductase, L-xylulose
-
-
-
-
additional information
-
enzyme belongs to the short-chain dehydrogenase/reductase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xylitol + NADP+ = L-xylulose + NADPH + H+
show the reaction diagram
enzyme with dual function showing L-xylulose reductase and dicarbonyl reductase activities
xylitol + NADP+ = L-xylulose + NADPH + H+
show the reaction diagram
enzyme with dual function showing L-xylulose reductase and dicarbonyl reductase activities, it is probably identical with sperm 34 kDa protein P34H and diacetyl reductase, EC 1.1.1.5, the amino acid residues Ser136, Tyr149, and Lys153 form the catalytic triad
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
xylitol:NADP+ 4-oxidoreductase (L-xylulose-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-17-5
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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
dicarbonyl reductase activity, best substrate, NADPH is the preferred cofactor, forward reaction is preferred
-
-
r
D-erythrose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
D-ribulose + NADPH
D-ribitol + NADP+
show the reaction diagram
reductase activity
-
-
r
D-threose + NADPH
D-threitol + NADP+
show the reaction diagram
reductase activity
-
-
r
D-xylulose + NADPH + H+
D-xylitol + NADP+
show the reaction diagram
reductase activity
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
DL-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
show the reaction diagram
reductase activity, forward reaction is highly preferred
-
-
r
L-erythrulose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
L-threose + NADPH
L-threitol + NADP+
show the reaction diagram
reductase activity
-
-
r
L-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
reductase activity
-
-
r
xylitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
1,4-dibromo-2,3-butanedione + NADPH
? + NADP+
show the reaction diagram
-
dicarbonyl reductase activity
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
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-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
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
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-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
preferred cofactor, reverse reaction
NADPH
preferred cofactor, forward reaction
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-hydroxybutyric acid
50% inhibition at 2.0 mM
acetoacetic acid
50% inhibition at 2.5 mM
heptanoic acid
50% inhibition at 2.5 mM
hexanoic acid
50% inhibition at 0.42 mM
n-butyric acid
50% inhibition at 0.052 mM
pentanoic acid
50% inhibition at 0.5 mM
propionic acid
50% inhibition at 0.13 mM
Pyruvic acid
50% inhibition at 1.0 mM
threonic acid
50% inhibition at 1.9 mM
4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide
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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
4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide
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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
n-butyric acid
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specific, binds to the enzyme-NADP+ complex, the mutant enzymes show altered sensitivity to inhibition, overview
additional information
acetic acid, oxaloacetic acid, and octanoic acid are poor inhibitors
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.9
acetoin
pH 7.0, 25°C
6
D-erythrose
pH 7.0, 25°C
6.3
D-ribulose
pH 7.0, 25°C
16
D-threitol
pH 7.0, 25°C
4
D-threose
pH 7.0, 25°C
18
D-xylulose
pH 7.0, 25°C
1.1
diacetyl
pH 7.0, 25°C
60
dihydroxyacetone
pH 7.0, 25°C
2.7
DL-glyceraldehyde
pH 7.0, 25°C
5.5
L-erythrulose
pH 7.0, 25°C
8.3
L-threose
pH 7.0, 25°C
0.23
L-xylulose
pH 7.0, 25°C
1.5
NAD+
pH 7.0, 25°C
0.36
NADH
pH 7.0, 25°C
0.003
NADP+
pH 7.0, 25°C
0.007
NADPH
pH 7.0, 25°C
11
xylitol
pH 7.0, 25°C
0.005 - 0.139
1,4-dibromo-2,3-butanedione
0.78 - 42
diacetyl
0.0099 - 0.085
L-xylitol
0.092 - 7.2
L-xylulose
0.00067 - 0.117
NADP+
0.002 - 0.053
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.9
acetoin
pH 7.0, 25°C
18
D-erythrose
pH 7.0, 25°C
19
D-ribulose
pH 7.0, 25°C
12
D-threitol
pH 7.0, 25°C
2 - 8
D-threose
pH 7.0, 25°C
18
D-xylulose
pH 7.0, 25°C
25
diacetyl
pH 7.0, 25°C
5.1
dihydroxyacetone
pH 7.0, 25°C
21
DL-glyceraldehyde
pH 7.0, 25°C
25
L-erythrulose
pH 7.0, 25°C
16
L-threose
pH 7.0, 25°C
39
L-xylulose
pH 7.0, 25°C
41
NAD+
pH 7.0, 25°C
23
NADH
pH 7.0, 25°C
10
NADP+
pH 7.0, 25°C
25
NADPH
pH 7.0, 25°C
10
xylitol
pH 7.0, 25°C
9.5
NADP+
-
pH 7.0, 25°C, wild-type enzyme
0.0005 - 25
NADPH
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
high content
Manually annotated by BRENDA team
high content
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCXR_RAT
244
0
25720
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26500
-
x * 26500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 26500
tetramer
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-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H146L
K153M
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site-directed mutagenesis, active site mutant, complete loss of activity
L143F
N190V
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site-directed mutagenesis, altered activity
N190V/W191S
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site-directed mutagenesis, almost complete loss of L-xylulose reductase activity
N190V/W191S/Q137M/L143F/H146L
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site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows high 3-ketosteroid reductase activity
Q137M
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site-directed mutagenesis, altered activity, stable against cold inactivation
Q137M/F241L
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site-directed mutagenesis, altered activity, sensitive to cold inactivation like the wild-type enzyme
Q137M/L143F
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site-directed mutagenesis, increased Km for L-xylulose compared to the wild-type
Q137M/L143F/H146L
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site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows 3-ketosteroid reductase activity
S136A
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site-directed mutagenesis, active site mutant, complete loss of activity
W191F
W191S
Y149F
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site-directed mutagenesis, active site mutant, complete loss of activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
rapidly dissociates into the inactive dimeric form at low temperature
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ishikura, S.; Isaji, T.; Usami, N.; Nakagawa, J.; El-Kabbani, O.; Hara, A.
Identification of amino acid residues involved in substrate recognition of L-xylulose reductase by site-directed mutagenesis
Chem. Biol. Interact.
143-144
543-550
2003
Rattus norvegicus
Manually annotated by BRENDA team
Nakagawa, J.; Ishikura, S.; Asami, J.; Isaji, T.; Usami, N.; Hara, A.; Sakurai, T.; Tsuritani, K.; Oda, K.; Takahashi, M.; Yoshimoto, M.; Otsuka, N.; Kitamura, K.
Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney
J. Biol. Chem.
277
17888-17891
2002
Cavia porcellus (Q920N9), Cavia porcellus, Homo sapiens (Q7Z4W1), Homo sapiens, Mesocricetus auratus (Q91XV4), Mus musculus (Q91X52), Mus musculus, Rattus norvegicus (Q920P0)
Manually annotated by BRENDA team
Matsunaga, T.; Shintani, S.; Hara, A.
Multiplicity of mammalian reductases for xenobiotic carbonyl compounds
Drug Metab. Pharmacokinet.
21
1-18
2006
Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
El-Kabbani, O.; Carbone, V.; Darmanin, C.; Ishikura, S.; Hara, A.
Structure of the tetrameric form of human L-xylulose reductase: probing the inhibitor-binding site with molecular modeling and site-directed mutagenesis
Proteins
60
424-432
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team