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Information on EC 1.1.1.10 - L-xylulose reductase and Organism(s) Mesocricetus auratus and UniProt Accession Q91XV4

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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:
Mesocricetus auratus
UNIPROT: Q91XV4 not found.
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The taxonomic range for the selected organisms is: Mesocricetus auratus
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
dicarbonyl/L-xylulose reductase
-
-
reductase, L-xylulose
-
-
-
-
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
immunological analysis revealed that the dicarbonyl/L-xylulose reductase is not identical with the sperm protein P26h
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
-
r
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 + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
reductase activity
-
-
r
L-xylulose + NADPH + H+
xylitol + NADP+
show the reaction diagram
-
-
-
r
xylitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
?
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 1.0 mM
acetoacetic acid
50% inhibition at 1.8 mM
heptanoic acid
50% inhibition at 1.4 mM
hexanoic acid
50% inhibition at 0.40 mM
n-butyric acid
50% inhibition at 0.026 mM
octanoic acid
50% inhibition at 2.5 mM
oxaloacetic acid
50% inhibition at 2.5 mM
pentanoic acid
50% inhibition at 0.20 mM
propionic acid
50% inhibition at 0.096 mM
Pyruvic acid
50% inhibition at 0.88 mM
threonic acid
50% inhibition at 0.75 mM
additional information
acetic acid is a poor inhibitor
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.3
acetoin
pH 7.0, 25°C
3.9
D-erythrose
pH 7.0, 25°C
6.3
D-ribulose
pH 7.0, 25°C
34
D-threitol
pH 7.0, 25°C
2.7
D-threose
pH 7.0, 25°C
12
D-xylulose
pH 7.0, 25°C
0.2
diacetyl
pH 7.0, 25°C
60
dihydroxyacetone
pH 7.0, 25°C
5.1
DL-glyceraldehyde
pH 7.0, 25°C
2.9
L-erythrulose
pH 7.0, 25°C
4.3
L-threose
pH 7.0, 25°C
0.26
L-xylulose
pH 7.0, 25°C
0.91
NAD+
pH 7.0, 25°C
0.12
NADH
pH 7.0, 25°C
0.003
NADP+
pH 7.0, 25°C
0.003
NADPH
pH 7.0, 25°C
40
xylitol
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.9
acetoin
pH 7.0, 25°C
23
D-erythrose
pH 7.0, 25°C
31
D-ribulose
pH 7.0, 25°C
16
D-threitol
pH 7.0, 25°C
31
D-threose
pH 7.0, 25°C
6.9
D-xylulose
pH 7.0, 25°C
30
diacetyl
pH 7.0, 25°C
8.7
dihydroxyacetone
pH 7.0, 25°C
22
DL-glyceraldehyde
pH 7.0, 25°C
25
L-erythrulose
pH 7.0, 25°C
23
L-threose
pH 7.0, 25°C
3 - 6
L-xylulose
pH 7.0, 25°C
44
NAD+
pH 7.0, 25°C
2 - 8
NADH
pH 7.0, 25°C
26
NADP+
pH 7.0, 25°C
27
NADPH
pH 7.0, 25°C
2 - 8
xylitol
pH 7.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
642
purified native enzyme, L-xylulose reductase activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
-
from caput, corpus, and cauda, activity in descending order
Manually annotated by BRENDA team
-
epididymal
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_MESAU
244
0
25675
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
x * 31000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 31000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli, native from liver
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Saint-Cyr, A.; Legare, C.; Frenette, G.; Gaudreault, C.; Sullivan, R.
P26h and dicarbonyl/L-xylulose reductase are two distinct proteins present in the hamster epididymis
Mol. Reprod. Dev.
69
137-145
2004
Mesocricetus auratus
Manually annotated by BRENDA team