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Information on EC 1.1.1.10 - L-xylulose reductase and Organism(s) Homo sapiens

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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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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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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
L-xylulose reductase
-
-
reductase, L-xylulose
-
-
-
-
additional information
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 SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
xylitol:NADP+ 4-oxidoreductase (L-xylulose-forming)
-
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 + NADH + H+
D-arabinitol + NAD+
show the reaction diagram
-
-
-
?
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
diacetyl + NADPH + H+
acetoin + NADP+
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
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
-
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
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-hydroxybutyric acid
50% inhibition at 1.1 mM
4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide
-
-
acetoacetic acid
50% inhibition at 0.63 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
heptanoic acid
50% inhibition at 0.38 mM
hexanoic acid
50% inhibition at 0.10 mM
n-butyric acid
oxaloacetic acid
50% inhibition at 0.91 mM
pentanoic acid
50% inhibition at 0.15 mM
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
50% inhibition at 0.38 mM
Pyruvic acid
50% inhibition at 0.50 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
acetoin
pH 7.0, 25°C
2.4
D-erythrose
pH 7.0, 25°C
5
D-ribulose
pH 7.0, 25°C
18
D-threitol
pH 7.0, 25°C
1.9
D-threose
pH 7.0, 25°C
4.8
D-xylulose
pH 7.0, 25°C
0.077 - 31
diacetyl
1.6
dihydroxyacetone
pH 7.0, 25°C
1.2
DL-glyceraldehyde
pH 7.0, 25°C
2.5
L-erythrulose
pH 7.0, 25°C
4.2
L-threose
pH 7.0, 25°C
0.21
L-xylulose
pH 7.0, 25°C
0.85
NAD+
pH 7.0, 25°C
0.17
NADH
pH 7.0, 25°C
0.001
NADP+
pH 7.0, 25°C
0.002 - 97
NADPH
25
xylitol
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65
acetoin
pH 7.0, 25°C
0.43
D-erythrose
pH 7.0, 25°C
0.52
D-ribulose
pH 7.0, 25°C
0.48
D-threitol
pH 7.0, 25°C
0.82
D-threose
pH 7.0, 25°C
0.1
D-xylulose
pH 7.0, 25°C
0.0008 - 1.6
diacetyl
0.23
dihydroxyacetone
pH 7.0, 25°C
0.52
DL-glyceraldehyde
pH 7.0, 25°C
0.6
L-erythrulose
pH 7.0, 25°C
0.52
L-threose
pH 7.0, 25°C
0.65
L-xylulose
pH 7.0, 25°C
1.5
NAD+
pH 7.0, 25°C
3.8
NADH
pH 7.0, 25°C
0.65
NADP+
pH 7.0, 25°C
1.5
NADPH
pH 7.0, 25°C
0.6
xylitol
pH 7.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00037 - 0.00044
4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
-
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
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_HUMAN
244
0
25913
Swiss-Prot
Mitochondrion (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
x-ray crystallography
tetramer
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N107D
site-directed mutagenesis, active site residue mutant, inactive
N107L
site-directed mutagenesis, active site residue mutant, inactive
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
stable at low temperatures
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
expression of wild-type and mutant enzymes in Escherichia coli
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
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
Carbone, V.; Darmanin, C.; Ishikura, S.; Hara, A.; El-Kabbani, O.
Structure-based design of inhibitors of human L-xylulose reductase modelled into the active site of the enzyme
Bioorg. Med. Chem. Lett.
13
1469-1474
2003
Homo sapiens
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
El-Kabbani, O.; Ishikura, S.; Darmanin, C.; Carbone, V.; Chung, R.P.T.; Usami, N.; Hara, A.
Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis
Proteins
55
724-732
2004
Homo sapiens (Q7Z4W1), Homo sapiens
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
Matsunaga, T.; Kamiya, T.; Sumi, D.; Kumagai, Y.; Kalyanaraman, B.; Hara, A.
L-Xylulose reductase is involved in 9,10-phenanthrenequinone-induced apoptosis in human T lymphoma cells
Free Radic. Biol. Med.
44
1191-1202
2008
Homo sapiens
Manually annotated by BRENDA team
Zhao, H.T.; Endo, S.; Ishikura, S.; Chung, R.; Hogg, P.J.; Hara, A.; El-Kabbani, O.
Structure/function analysis of a critical disulfide bond in the active site of L-xylulose reductase
Cell. Mol. Life Sci.
66
1570-1579
2009
Homo sapiens (Q7Z4W1)
Manually annotated by BRENDA team