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Information on EC 1.1.1.10 - L-xylulose reductase and Organism(s) Mus musculus and UniProt Accession Q91X52

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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:
Mus musculus
UNIPROT: Q91X52 not found.
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The taxonomic range for the selected organisms is: Mus musculus
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, rplxr3, nadp(+)-dependent xylitol dehydrogenase, 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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
-
reduction
-
-
-
-
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
-
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
DL-threitol + NAD+
D-threose + NADH
show the reaction diagram
-
-
-
?
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
xylitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
-
dicarbonyl reductase activity
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
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
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
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uronate cycle of glucose metabolism
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
preferred cofactor, reverse reaction
NADPH
preferred cofactor, forward reaction
NADP+
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heptanoic acid
50% inhibition at 2.0 mM
hexanoic acid
50% inhibition at 1.1 mM
n-butyric acid
50% inhibition at 0.05 mM
oxaloacetic acid
50% inhibition at 2.5 mM
pentanoic acid
50% inhibition at 0.38 mM
propionic acid
50% inhibition at 0.17 mM
Pyruvic acid
50% inhibition at 1.5 mM
threonic acid
50% inhibition at 1.5 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9
acetoin
pH 7.0, 25°C
5.7
D-erythrose
pH 7.0, 25°C
5.7
D-ribulose
pH 7.0, 25°C
37
D-threitol
pH 7.0, 25°C
2.4
D-threose
pH 7.0, 25°C
12
D-xylulose
pH 7.0, 25°C
0.67
diacetyl
pH 7.0, 25°C
47
dihydroxyacetone
pH 7.0, 25°C
6
DL-glyceraldehyde
pH 7.0, 25°C
4.8
L-erythrulose
pH 7.0, 25°C
5.6
L-threose
pH 7.0, 25°C
0.24
L-xylulose
pH 7.0, 25°C
0.99
NAD+
pH 7.0, 25°C
0.22
NADH
pH 7.0, 25°C
0.003
NADP+
pH 7.0, 25°C
0.005
NADPH
pH 7.0, 25°C
15
xylitol
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
acetoin
pH 7.0, 25°C
18
D-erythrose
pH 7.0, 25°C
26
D-ribulose
pH 7.0, 25°C
16
D-threitol
pH 7.0, 25°C
23
D-threose
pH 7.0, 25°C
7.4
D-xylulose
pH 7.0, 25°C
41
diacetyl
pH 7.0, 25°C
3.3
dihydroxyacetone
pH 7.0, 25°C
24
DL-glyceraldehyde
pH 7.0, 25°C
23
L-erythrulose
pH 7.0, 25°C
16
L-threose
pH 7.0, 25°C
37
L-xylulose
pH 7.0, 25°C
55
NAD+
pH 7.0, 25°C
41
NADH
pH 7.0, 25°C
15
NADP+
pH 7.0, 25°C
34
NADPH
pH 7.0, 25°C
17
xylitol
pH 7.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
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
high content
Manually annotated by BRENDA team
low expression level
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCXR_MOUSE
244
0
25746
Swiss-Prot
Mitochondrion (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
-
the dimeric form is inactive
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D238E
-
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
D238E/L242W
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site-directed mutagenesis, mutation leads to complete prevention of cold inactivation, mutant exists in tetrameric form at low temperature
D238E/L242W/T244C
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site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
L242W
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site-directed mutagenesis, mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
L242W/T244C
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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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ishikura, S.; Usami, N.; El-Kabbani, O.; Hara, A.
Structural determinant for cold inactivation of rodent L-xylulose reductase
Biochem. Biophys. Res. Commun.
308
68-72
2003
Homo sapiens, Mus musculus
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
Sudo, T.; Ishii, A.; Asami, J.; Uematsu, Y.; Saitoh, M.; Nakamura, A.; Tada, N.; Ohnuki, T.; Komurasaki, T.; Nakagawa, J.
Transgenic mice over-expressing dicarbonyl/L-xylulose reductase gene crossed with KK-A(y) diabetic model mice: an animal model for the metabolism of renal carbonyl compounds
Exp. Anim.
54
385-394
2005
Mus musculus
Manually annotated by BRENDA team