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
1.1.1.10
-
RECOMMENDED NAME
GeneOntology No.
L-xylulose reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
xylitol + NADP+ = L-xylulose + NADPH + H+
show the reaction diagram
probably identical with EC 1.1.1.5 diacetyl reductase
-
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
-
xylitol + NADP+ = L-xylulose + NADPH + H+
show the reaction diagram
active site structure
-
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
-
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
-
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
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
-
xylitol + NADP+ = L-xylulose + NADPH + H+
show the reaction diagram
active site residues are Cys138, Val143, His146, Trp191, and Met200, the catalytic tetrad is formed by Asn107, Ser136, Tyr149, and Lys153, substrate binding site structure, enzyme with dual function showing L-xylulose reductase activity and dicarbonyl reductase activity, EC 1.1.1.5
-
xylitol + NADP+ = L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-glucuronate degradation I
-
-
L-arabinose degradation II
-
-
Pentose and glucuronate interconversions
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
xylitol:NADP+ 4-oxidoreductase (L-xylulose-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dicarbonyl/L-xylulose reductase
-
dicarbonyl/L-xylulose reductase
-
-
L-xylulose reductase
-
-
L-xylulose reductase
-
L-xylulose reductase
-
-
NAD(P)H-dependent xylose reductase
-
-
NAD(P)H-dependent xylose reductase
-
-
NADP(+)-dependent xylitol dehydrogenase
-
-
reductase, L-xylulose
-
-
-
-
xylitol dehydrogenase
-
-
xylose reductase
Meyerozyma guilliermondii FTI, Meyerozyma guilliermondii FTI 20037
-
-
-
xylose reductase
-
-
additional information
-
xylitol:NAD+ 2-oxidoreductase, EC 1.1.1.9, is termed as xylitol dehydrogenase
additional information
-
enzyme belongs to the short-chain dehydrogenase/reductase family
additional information
-
enzyme belongs to the short-chain dehydrogenase/reductase family
additional information
-
enzyme belongs to the short-chain dehydrogenase/reductase family
CAS REGISTRY NUMBER
COMMENTARY
9028-17-5
-
ORGANISM
COMMENTARY
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
strain 4D2P
-
-
Manually annotated by BRENDA team
Erwinia sp. 4D2P
strain 4D2P
-
-
Manually annotated by BRENDA team
male golden hamster, 3 and 8 weeks old
-
-
Manually annotated by BRENDA team
Meyerozyma guilliermondii FTI
strain FTI
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
xylitol utilizing mutant strains, e.g. DM101, of strain 19321
-
-
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
LITERATURE
evolution
L-xylulose reductases belong to the superfamily of short chain dehydrogenases and reductases (SDRs)
evolution
-
L-xylulose reductases belong to the superfamily of short chain dehydrogenases and reductases (SDRs)
-
malfunction
deletion of lxr3 affects growth on L-arabinose and L-arabitol and reduces total NADPH-dependent LXR activity in cell free extracts
malfunction
dhs-21 null mutants show defects in longevity, reproduction and egg-laying
malfunction
-
deletion of lxr3 affects growth on L-arabinose and L-arabitol and reduces total NADPH-dependent LXR activity in cell free extracts
-
metabolism
the enzyme catalyzes the NADPH-dependent reduction of L-xylulose to xylitol in L-arabinose and glucuronic acid catabolism
metabolism
dicarbonyl/L-xylulose reductase converts L-xylulose into xylitol, and reduces various alpha-dicarbonyl compounds, performing a dual role in carbohydrate metabolism and detoxification
metabolism
-
the enzyme catalyzes the NADPH-dependent reduction of L-xylulose to xylitol in L-arabinose and glucuronic acid catabolism
-
physiological function
-
deletion results in a strain lacking the NADPH-specific L-xylulose reductase activity and having reduced growth on L-arabinose
physiological function
the L-xylulose reductase is essential for L-arabinose catabolism in Trichoderma reesei
physiological function
the enzyme is essential for normal life span and reproduction
physiological function
-
the L-xylulose reductase is essential for L-arabinose catabolism in Trichoderma reesei
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
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
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
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
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
1,4-dibromo-2,3-butanedione + NADPH
? + NADP+
show the reaction diagram
-
dicarbonyl reductase activity
-
r
D-erythrose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
D-erythrose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
D-erythrose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
D-erythrose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
D-erythrose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
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
D-ribitol + NADP+
show the reaction diagram
reductase activity
-
r
D-ribulose + NADPH
D-ribitol + NADP+
show the reaction diagram
reductase activity
-
r
D-ribulose + NADPH
D-ribitol + NADP+
show the reaction diagram
reductase activity
-
r
D-ribulose + NADPH
D-ribitol + NADP+
show the reaction diagram
reductase activity
-
r
D-ribulose + NADPH
D-ribitol + NADP+
show the reaction diagram
reductase activity
-
r
D-ribulose + NADPH + H+
D-ribitol + NADP+
show the reaction diagram
-
-
-
?
D-ribulose + NADPH + H+
? + 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
reductase activity
-
r
D-threose + NADPH
D-threitol + NADP+
show the reaction diagram
reductase activity
-
r
D-threose + NADPH
D-threitol + NADP+
show the reaction diagram
reductase activity
-
r
D-threose + NADPH
D-threitol + NADP+
show the reaction diagram
reductase activity
-
r
D-threose + NADPH
D-threitol + NADP+
show the reaction diagram
reductase activity
-
r
D-threose + NADPH + H+
? + NADP+
show the reaction diagram
-
-
ir
D-xylulose + NADH + H+
D-arabinitol + NAD+
show the reaction diagram
-
-
-
D-xylulose + NADH + H+
D-arabinitol + NAD+
show the reaction diagram
about 100fold lower activity compared to L-xylulose
-
r
D-xylulose + NADPH + H+
D-xylitol + NADP+
show the reaction diagram
reductase activity
-
r
D-xylulose + NADPH + H+
D-xylitol + NADP+
show the reaction diagram
reductase activity
-
r
D-xylulose + NADPH + H+
D-xylitol + NADP+
show the reaction diagram
reductase activity
-
r
D-xylulose + NADPH + H+
D-xylitol + NADP+
show the reaction diagram
reductase activity
-
r
D-xylulose + NADPH + H+
D-xylitol + NADP+
show the reaction diagram
reductase activity
-
r
D-xylulose + NADPH + H+
xylitol + NADP+
show the reaction diagram
-
-
?
D-xylulose + NADPH + H+
xylitol + NADP+
show the reaction diagram
low activity
-
?
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
-
-
-
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
-
-
-
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
-
detoxification of alpha-dicarbonyl compounds
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
-
dicarbonyl reductase activity
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
-
dicarbonyl reductase activity
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
-
dicarbonyl reductase activity
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
r
diacetyl + NAD(P)H
acetoin + NAD(P)+
show the reaction diagram
dicarbonyl reductase activity, NADPH is the preferred cofactor
-
r
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-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
show the reaction diagram
reductase activity, forward reaction is highly preferred
-
r
DL-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
show the reaction diagram
reductase activity, forward reaction is highly preferred
-
r
DL-glyceraldehyde + NADPH
dihydroxyacetone + NADP+
show the reaction diagram
reductase activity, forward reaction is highly preferred
-
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
-
-
-
DL-threitol + NAD+
D-threose + NADH
show the reaction diagram
-
-
-
DL-threitol + NAD+
D-threose + NADH
show the reaction diagram
-
-
-
DL-threitol + NAD+
D-threose + NADH
show the reaction diagram
-
-
-
r
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
reductase activity
-
-
r
L-erythrulose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
L-erythrulose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
L-erythrulose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
L-erythrulose + NADPH
?
show the reaction diagram
reductase activity
-
-
r
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
low activity
-
?
L-threose + NADPH
L-threitol + NADP+
show the reaction diagram
reductase activity
-
r
L-threose + NADPH
L-threitol + NADP+
show the reaction diagram
reductase activity
-
r
L-threose + NADPH
L-threitol + NADP+
show the reaction diagram
reductase activity
-
r
L-threose + NADPH
L-threitol + NADP+
show the reaction diagram
reductase activity
-
r
L-threose + NADPH
L-threitol + NADP+
show the reaction diagram
reductase activity
-
r
L-xylulose + NADH
L-xylitol + NAD+
show the reaction diagram
-
-
r
L-xylulose + NADH
L-xylitol + NAD+
show the reaction diagram
part of the L-arabinose catabolism
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
-
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
also reduces 2,3-butadione
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
part of the glucuronic acid pathway, enzyme may be involved in water reabsorption and cellular osmoregulation
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
part of the uronate cycle, involved in osmoregulation in the kidney
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
the enzyme is involved in the uronate cycle of glucose metabolism, L-xylulose reductase activity
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
L-xylulose reductase activity
-
r
L-xylulose + NADPH + H+
L-xylitol + 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+
L-xylitol + 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+
L-xylitol + NADP+
show the reaction diagram
reductase activity
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
uronate cycle of glucose metabolism
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
xylulose reductase has about 50% higher activity during xylose consumption than during the coconsumption of glucose and xylose
-
?
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
Meyerozyma guilliermondii FTI, Meyerozyma guilliermondii FTI 20037
-
-
-
?
L-xylulose + NADPH + H+
xylitol + NADP+
show the reaction diagram
-
-
ir
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
?
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
?
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
r
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
strain DM101 and DM122, product identification is not exact, could also be D-xylulose
?
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
Erwinia sp. 4D2P
-
-
-
?
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
-
-
r
L-xylulose + NADPH + H+
xylitol + NADP+
show the reaction diagram
preferred substrate
-
r
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
-
minimal reductive activity also with D-xylulose, D-erythrose and dihydroxyacetone
-
-
-
additional information
?
-
-
no activity in the mitochondrial fraction with D-xylulose, D-sorbose, L-sorbose, L-erythrulose, D-fructose, D-sorbitol, L-arabitol, D-gulitol, D-talitol
-
-
-
additional information
?
-
-
minimal oxidative activity with D-arabitol, mannitol, 1,2-propanediol and 2,3-butanediol
-
-
-
additional information
?
-
NADH-linked enzyme form, no activity with NADPH and NADP+, no activity with L-arabinitol, adonitol or ribitol, dulcitol or galactitol, D-mannitol, and D-sorbitol, no activity with D-sorbose, L-sorbose, D-psicose, and D-fructose
-
-
-
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
-
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
-
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
-
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
-
additional information
?
-
substrate specificity for dicarbonyl reductase activity, overview
-
-
-
additional information
?
-
-
the size and hydrophobicity of the amino acid residues involved in substrate recognition, i.e. Q137, L143, H146, N190, and W191, is important, mutants N190V, N190V/W191S, Q137M/L143F/H146L, and N190V/W191S/Q137M/L143F/H146L show reductive activity with 4-nitroacetophenone, 5beta-androstane-3,17-dione, 5beta-androstan-17beta-ol-3-one, and 5beta-androstane-3alpha,17beta-diol, overview
-
-
-
additional information
?
-
-
no substrate: D-fructose, D-sorbose, L-sorbose, xylitol, D-arabitol, L-arabitol, ribitol, D-sorbitol and galactitol
-
-
-
additional information
?
-
dicarbonyl/L-xylulose reductase is bifunctional
-
-
-
additional information
?
-
substrate specificity, overview. No activity with L-xylo-3-hexulose, D-sorbose, D-ribitol, D-arabitol, or L-arabitol
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
part of the glucuronic acid pathway, enzyme may be involved in water reabsorption and cellular osmoregulation
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
part of the uronate cycle, involved in osmoregulation in the kidney
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
the enzyme is involved in the uronate cycle of glucose metabolism
-
r
L-xylulose + NADPH + H+
L-xylitol + NADP+
show the reaction diagram
-
uronate cycle of glucose metabolism
-
?
xylitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
G0RH19
-
-
r
L-xylulose + NADPH + H+
xylitol + NADP+
show the reaction diagram
Q21929
-
-
ir
additional information
?
-
Q21929
dicarbonyl/L-xylulose reductase is bifunctional
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
preference for, coenzyme-binding domain is a beta-alpha-beta-fold typical for NAD+ dehydrogenases
NAD+
-
much less effective than NADP+
NAD+
-
no activity with
NAD+
-
preference for, coenzyme-binding domain is a beta-alpha-beta-fold typical for NAD+ dehydrogenases
NAD+
-
-
NAD+
specific for, no activity with NADP+
NADH
-
-
NADH
specific for no activity with NADPH
NADP+
-
B-specific hydrogen transfer from xylitol to NADP+
NADP+
-
much more effective than NAD+
NADP+
-
-
NADP+
preferred cofactor, reverse reaction
NADP+
-
preferred cofactor, reverse reaction
NADP+
preferred cofactor, reverse reaction
NADP+
preferred cofactor, reverse reaction
NADP+
preferred cofactor, reverse reaction
NADP+
-
binding structure determination
NADPH
-
preference for
NADPH
preferred cofactor, forward reaction
NADPH
-
preferred cofactor, forward reaction
NADPH
preferred cofactor, forward reaction
NADPH
preferred cofactor, forward reaction
NADPH
preferred cofactor, forward reaction
NADPH
-
binding structure determination
NADPH
-
-
NADPH
-
has a higher affinity for NADPH than for NADH
additional information
-
-
-
additional information
-
determination of Ki of NADP+ and NADPH in competition with each other
-
additional information
-
the enzyme does not accept NAD+
-
additional information
-
no activitiy with NADH
-
additional information
no activity with NADH
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-hydroxybutyric acid
-
50% inhibition at 1.1 mM
3-hydroxybutyric acid
50% inhibition at 1.0 mM
3-hydroxybutyric acid
50% inhibition at 2.0 mM
4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide
-
-
4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide
-
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
-
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
-
50% inhibition at 0.63 mM
acetoacetic acid
50% inhibition at 1.8 mM
acetoacetic acid
50% inhibition at 2.5 mM
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
-
50% inhibition at 0.38 mM
heptanoic acid
50% inhibition at 1.4 mM
heptanoic acid
50% inhibition at 2.0 mM
heptanoic acid
50% inhibition at 2.5 mM
hexanoic acid
-
50% inhibition at 0.10 mM
hexanoic acid
50% inhibition at 0.40 mM
hexanoic acid
50% inhibition at 1.1 mM
hexanoic acid
50% inhibition at 0.42 mM
iodoacetate
-
not inhibitory
n-butyric acid
-
binds to the active site of the enzyme, complex structure determination and analysis
n-butyric acid
-
specific, binds to the enzyme-NADP+ complex, the mutant enzymes show altered sensitivity to inhibition, overview
n-butyric acid
-
50% inhibition at 0.064 mM
n-butyric acid
50% inhibition at 0.026 mM
n-butyric acid
50% inhibition at 0.05 mM
n-butyric acid
50% inhibition at 0.052 mM
Octanoic acid
50% inhibition at 2.5 mM
oxaloacetic acid
-
50% inhibition at 0.91 mM
oxaloacetic acid
50% inhibition at 2.5 mM
oxaloacetic acid
50% inhibition at 2.5 mM
p-chloromercuribenzoate
-
-
pentanoic acid
-
50% inhibition at 0.15 mM
pentanoic acid
50% inhibition at 0.20 mM
pentanoic acid
50% inhibition at 0.38 mM
pentanoic acid
50% inhibition at 0.5 mM
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
-
50% inhibition at 0.38 mM
Propionic acid
50% inhibition at 0.096 mM
Propionic acid
50% inhibition at 0.17 mM
Propionic acid
50% inhibition at 0.13 mM
Pyruvic acid
-
50% inhibition at 0.50 mM
Pyruvic acid
50% inhibition at 0.88 mM
Pyruvic acid
50% inhibition at 1.5 mM
Pyruvic acid
50% inhibition at 1.0 mM
threonic acid
50% inhibition at 0.75 mM
threonic acid
50% inhibition at 1.5 mM
threonic acid
50% inhibition at 1.9 mM
iodoacetate
-
complete inhibition of L-xylulose reductive activity at 5 mM
additional information
-
not: EDTA
-
additional information
-
modelling of structure-based inhibitor binding into the active site
-
additional information
-
acetic acid, threonic acid, and octanoic acid are poor inhibitors
-
additional information
acetic acid is a poor inhibitor
-
additional information
acetic acid, acetoacetic acid, 3-OH-butyric acid, and octanoic acid are poor inhibitors
-
additional information
acetic acid, oxaloacetic acid, and octanoic acid are poor inhibitors
-
additional information
-
the level of xylose reductase decreases when the initial xylose concentration is increased from 30 to 70 g/l
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
1,4-dibromo-2,3-butanedione
-
pH 7.0, 25C, wild-type enzyme
0.05
1,4-dibromo-2,3-butanedione
-
pH 7.0, 25C, mutant S136A
0.1
1,4-dibromo-2,3-butanedione
-
pH 7.0, 25C, mutant K153M
0.139
1,4-dibromo-2,3-butanedione
-
pH 7.0, 25C, mutant Y149F
1.5
acetoin
-
pH 7.0, 25C
3.3
acetoin
pH 7.0, 25C
6.9
acetoin
pH 7.0, 25C
9
acetoin
pH 7.0, 25C
13
acetoin
pH 7.0, 25C
2.7
D-arabinitol
pH 9.0, 30C, purified recombinant enzyme
0.27
D-erythrose
pH 7.0, temperature not specified in the publication
0.59
D-erythrose
pH 7.0, 25C
2.4
D-erythrose
-
pH 7.0, 25C
3.9
D-erythrose
pH 7.0, 25C
5.7
D-erythrose
pH 7.0, 25C
6
D-erythrose
pH 7.0, 25C
4.7
D-ribulose
pH 7.0, 30C, purified recombinant enzyme
5
D-ribulose
-
pH 7.0, 25C
5.7
D-ribulose
pH 7.0, 25C
6.3
D-ribulose
pH 7.0, 25C
6.3
D-ribulose
pH 7.0, 25C
7.8
D-ribulose
pH 7.0, 25C
105
D-ribulose
pH 7.0, 30C, recombinant enzyme
150
D-ribulose
-
-
250
D-sorbitol
pH 7.0, 30C, recombinant enzyme
14
D-threitol
pH 7.0, 25C
16
D-threitol
pH 7.0, 25C
18
D-threitol
-
pH 7.0, 25C
34
D-threitol
pH 7.0, 25C
37
D-threitol
pH 7.0, 25C
0.68
D-threose
pH 7.0, temperature not specified in the publication
1.9
D-threose
-
pH 7.0, 25C
2
D-threose
pH 7.0, 25C
2.4
D-threose
pH 7.0, 25C
2.7
D-threose
pH 7.0, 25C
4
D-threose
pH 7.0, 25C
2.58
D-xylulose
pH 7.0, temperature not specified in the publication
4.8
D-xylulose
-
pH 7.0, 25C
12
D-xylulose
pH 7.0, 25C
12
D-xylulose
pH 7.0, 25C
18
D-xylulose
pH 7.0, 25C
18
D-xylulose
pH 7.0, 25C
0.077
diacetyl
-
pH 7.0, 25C
0.077
diacetyl
-
pH 7.0, 25C, wild-type enzyme
0.0945
diacetyl
-
wild type enzyme, in 10 mM potassium phosphate buffer
0.2
diacetyl
pH 7.0, 25C
0.22
diacetyl
-
mutant enzyme C138A, in 10 mM potassium phosphate buffer
0.52
diacetyl
pH 7.0, 25C
0.67
diacetyl
pH 7.0, 25C
0.78
diacetyl
-
pH 7.0, 25C, wild-type enzyme
1.1
diacetyl
pH 7.0, 25C
1.2
diacetyl
-
pH 7.0, 25C, mutant H146L
2.6
diacetyl
-
pH 7.0, 25C, mutant N190V
2.7
diacetyl
-
pH 7.0, 25C, mutant N190V/W191S/Q137M/L143F/H146L
3
diacetyl
-
pH 7.0, 25C, mutant Q137M
5.2
diacetyl
-
pH 7.0, 25C, mutant W191F
6.2
diacetyl
-
pH 7.0, 25C, mutant L143F
9.6
diacetyl
-
pH 7.0, 25C, mutant Q137M/L143F/H146L
11
diacetyl
-
pH 7.0, 25C, mutant Q137M/L143F
16
diacetyl
-
pH 7.0, 25C, mutant N190V/W191S
26
diacetyl
-
pH 7.0, 25C, mutant N107D
31
diacetyl
-
pH 7.0, 25C, mutant N107L
42
diacetyl
-
pH 7.0, 25C, mutant W191S
1.6
dihydroxyacetone
-
pH 7.0, 25C
36
dihydroxyacetone
pH 7.0, 25C
47
dihydroxyacetone
pH 7.0, 25C
60
dihydroxyacetone
pH 7.0, 25C
60
dihydroxyacetone
pH 7.0, 25C
1.2
DL-glyceraldehyde
-
pH 7.0, 25C
1.4
DL-glyceraldehyde
pH 7.0, 25C
2.7
DL-glyceraldehyde
pH 7.0, 25C
5.1
DL-glyceraldehyde
pH 7.0, 25C
6
DL-glyceraldehyde
pH 7.0, 25C
0.17
L-erythrulose
pH 7.0, temperature not specified in the publication
2
L-erythrulose
pH 7.0, 25C
2.5
L-erythrulose
-
pH 7.0, 25C
2.9
L-erythrulose
pH 7.0, 25C
4.8
L-erythrulose
pH 7.0, 25C
5.5
L-erythrulose
pH 7.0, 25C
0.18
L-ribulose
pH 7.0, temperature not specified in the publication
2.9
L-threose
pH 7.0, 25C
4.2
L-threose
-
pH 7.0, 25C
4.3
L-threose
pH 7.0, 25C
5.6
L-threose
pH 7.0, 25C
8.3
L-threose
pH 7.0, 25C
0.0099
L-xylitol
-
pH 7.0, 25C, mutant Y149F
0.011
L-xylitol
-
pH 7.0, 25C, wild-type enzyme
0.013
L-xylitol
-
pH 7.0, 25C, mutant S136A
0.085
L-xylitol
-
pH 7.0, 25C, mutant K153M
7.2
L-xylitol
pH 9.0, 30C, purified recombinant enzyme
0.05
L-xylulose
pH 7.0, 25C
0.092
L-xylulose
-
pH 7.0, 25C, mutant H146L
0.14
L-xylulose
-
pH 7.0, 25C, wild-type enzyme and mutant L143F
0.21
L-xylulose
-
pH 7.0, 25C
0.23
L-xylulose
pH 7.0, 25C
0.24
L-xylulose
pH 7.0, 25C
0.26
L-xylulose
pH 7.0, 25C
0.29
L-xylulose
-
-
0.31
L-xylulose
-
pH 7.0, 25C, mutant N190V
0.33
L-xylulose
-
pH 7.0, 25C, mutant Q137M
0.66
L-xylulose
pH 7.0, temperature not specified in the publication
3.6
L-xylulose
-
pH 7.0, 25C, mutant Q137M/L143F
7.2
L-xylulose
-
pH 7.0, 25C, mutant W191F
9.6
L-xylulose
pH 7.0, 30C, purified recombinant enzyme
16
L-xylulose
pH 7.0, 30C, recombinant enzyme
17
L-xylulose
-
-
25
L-xylulose
-
pH 7.0, 22C
0.85
NAD+
-
pH 7.0, 25C
0.91
NAD+
pH 7.0, 25C
0.99
NAD+
pH 7.0, 25C
1.5
NAD+
pH 7.0, 25C
0.12
NADH
pH 7.0, 25C
0.17
NADH
-
pH 7.0, 25C
0.22
NADH
pH 7.0, 25C
0.36
NADH
pH 7.0, 25C
0.69
NADH
pH 7.0, 25C
0.00067
NADP+
-
pH 7.0, 25C, mutant S136A
0.001
NADP+
-
pH 7.0, 25C
0.0013
NADP+
-
pH 7.0, 25C, mutant Y149F
0.002
NADP+
pH 7.0, 25C
0.003
NADP+
-
pH 7.0, 25C, wild-type enzyme
0.003
NADP+
pH 7.0, 25C
0.003
NADP+
pH 7.0, 25C
0.003
NADP+
pH 7.0, 25C
0.117
NADP+
-
pH 7.0, 25C, mutant K153M
0.13
NADP+
-
-
0.153
NADP+
-
-
0.002
NADPH
-
pH 7.0, 25C, mutant Y149F
0.002
NADPH
-
pH 7.0, 25C
0.002
NADPH
-
pH 7.0, 25C, wild-type enzyme
0.0026
NADPH
-
-
0.003
NADPH
pH 7.0, 25C
0.0046
NADPH
-
pH 7.0, 25C, mutant S136A
0.005
NADPH
pH 7.0, 25C
0.005
NADPH
pH 7.0, 25C
0.007
NADPH
-
pH 7.0, 25C, wild-type enzyme
0.007
NADPH
pH 7.0, 25C
0.03
NADPH
-
-
0.053
NADPH
-
pH 7.0, 25C, mutant K153M
0.13
NADPH
pH 7.0, 30C, recombinant enzyme, with L-xylulose
95
NADPH
-
pH 7.0, 25C, mutant N107D
97
NADPH
-
pH 7.0, 25C, mutant N107L
10
xylitol
pH 7.0, 25C
11
xylitol
pH 7.0, 25C
15
xylitol
pH 7.0, 25C
25
xylitol
-
pH 7.0, 25C
40
xylitol
pH 7.0, 25C
48
xylitol
-
-
72
xylitol
-
-
100
xylitol
pH 7.0, 30C, recombinant enzyme
925
xylitol
-
-
1239
xylitol
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.65
acetoin
Homo sapiens
-
pH 7.0, 25C
3
acetoin
Mus musculus
Q91X52
pH 7.0, 25C
6.9
acetoin
Cavia porcellus
Q920N9
pH 7.0, 25C
6.9
acetoin
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
6.9
acetoin
Rattus norvegicus
Q920P0
pH 7.0, 25C
0.43
D-erythrose
Homo sapiens
-
pH 7.0, 25C
1.8
D-erythrose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
2 - 8
D-erythrose
Cavia porcellus
Q920N9
pH 7.0, 25C
18
D-erythrose
Mus musculus
Q91X52
pH 7.0, 25C
18
D-erythrose
Rattus norvegicus
Q920P0
pH 7.0, 25C
23
D-erythrose
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
0.52
D-ribulose
Homo sapiens
-
pH 7.0, 25C
7.8
D-ribulose
Cavia porcellus
Q920N9
pH 7.0, 25C
8.24
D-ribulose
Trichoderma reesei
G0RH19
pH 7.0, 30C, recombinant enzyme
19
D-ribulose
Rattus norvegicus
Q920P0
pH 7.0, 25C
26
D-ribulose
Mus musculus
Q91X52
pH 7.0, 25C
31
D-ribulose
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
119
D-ribulose
Neurospora crassa
-
-
1.8
D-sorbitol
Trichoderma reesei
G0RH19
pH 7.0, 30C, recombinant enzyme
0.48
D-threitol
Homo sapiens
-
pH 7.0, 25C
12
D-threitol
Rattus norvegicus
Q920P0
pH 7.0, 25C
15
D-threitol
Cavia porcellus
Q920N9
pH 7.0, 25C
16
D-threitol
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
16
D-threitol
Mus musculus
Q91X52
pH 7.0, 25C
0.82
D-threose
Homo sapiens
-
pH 7.0, 25C
2 - 8
D-threose
Rattus norvegicus
Q920P0
pH 7.0, 25C
2.32
D-threose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
23
D-threose
Mus musculus
Q91X52
pH 7.0, 25C
31
D-threose
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
32
D-threose
Cavia porcellus
Q920N9
pH 7.0, 25C
0.1
D-xylulose
Homo sapiens
-
pH 7.0, 25C
1.22
D-xylulose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
6.9
D-xylulose
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
7.4
D-xylulose
Mus musculus
Q91X52
pH 7.0, 25C
18
D-xylulose
Rattus norvegicus
Q920P0
pH 7.0, 25C
19
D-xylulose
Cavia porcellus
Q920N9
pH 7.0, 25C
0.0008
diacetyl
Homo sapiens
-
pH 7.0, 25C, mutant N107L
0.009
diacetyl
Homo sapiens
-
pH 7.0, 25C, mutant N107D
1.57
diacetyl
Homo sapiens
-
pH 7.0, 25C, wild-type enzyme
1.6
diacetyl
Homo sapiens
-
pH 7.0, 25C
24
diacetyl
Cavia porcellus
Q920N9
pH 7.0, 25C
25
diacetyl
Rattus norvegicus
Q920P0
pH 7.0, 25C
30
diacetyl
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
41
diacetyl
Mus musculus
Q91X52
pH 7.0, 25C
0.23
dihydroxyacetone
Homo sapiens
-
pH 7.0, 25C
3.3
dihydroxyacetone
Mus musculus
Q91X52
pH 7.0, 25C
3.8
dihydroxyacetone
Cavia porcellus
Q920N9
pH 7.0, 25C
5.1
dihydroxyacetone
Rattus norvegicus
Q920P0
pH 7.0, 25C
8.7
dihydroxyacetone
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
0.52
DL-glyceraldehyde
Homo sapiens
-
pH 7.0, 25C
20
DL-glyceraldehyde
Cavia porcellus
Q920N9
pH 7.0, 25C
21
DL-glyceraldehyde
Rattus norvegicus
Q920P0
pH 7.0, 25C
22
DL-glyceraldehyde
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
24
DL-glyceraldehyde
Mus musculus
Q91X52
pH 7.0, 25C
0.6
L-erythrulose
Homo sapiens
-
pH 7.0, 25C
3.32
L-erythrulose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
23
L-erythrulose
Mus musculus
Q91X52
pH 7.0, 25C
24
L-erythrulose
Cavia porcellus
Q920N9
pH 7.0, 25C
25
L-erythrulose
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
25
L-erythrulose
Rattus norvegicus
Q920P0
pH 7.0, 25C
0.49
L-ribulose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
0.52
L-threose
Homo sapiens
-
pH 7.0, 25C
16
L-threose
Mus musculus
Q91X52
pH 7.0, 25C
16
L-threose
Rattus norvegicus
Q920P0
pH 7.0, 25C
23
L-threose
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
27
L-threose
Cavia porcellus
Q920N9
pH 7.0, 25C
0.65
L-xylulose
Homo sapiens
-
pH 7.0, 25C
3 - 6
L-xylulose
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
4.98
L-xylulose
Caenorhabditis elegans
Q21929
pH 7.0, temperature not specified in the publication
11.4
L-xylulose
Trichoderma reesei
G0RH19
pH 7.0, 30C, recombinant enzyme
37
L-xylulose
Cavia porcellus
Q920N9
pH 7.0, 25C
37
L-xylulose
Mus musculus
Q91X52
pH 7.0, 25C
39
L-xylulose
Rattus norvegicus
Q920P0
pH 7.0, 25C
1.5
NAD+
Homo sapiens
-
pH 7.0, 25C
41
NAD+
Rattus norvegicus
Q920P0
pH 7.0, 25C
44
NAD+
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
55
NAD+
Mus musculus
Q91X52
pH 7.0, 25C
2 - 8
NADH
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
3.8
NADH
Homo sapiens
-
pH 7.0, 25C
23
NADH
Rattus norvegicus
Q920P0
pH 7.0, 25C
41
NADH
Mus musculus
Q91X52
pH 7.0, 25C
76
NADH
Cavia porcellus
Q920N9
pH 7.0, 25C
0.65
NADP+
Homo sapiens
-
pH 7.0, 25C
9.5
NADP+
Rattus norvegicus
-
pH 7.0, 25C, wild-type enzyme
10
NADP+
Rattus norvegicus
Q920P0
pH 7.0, 25C
15
NADP+
Mus musculus
Q91X52
pH 7.0, 25C
23
NADP+
Cavia porcellus
Q920N9
pH 7.0, 25C
26
NADP+
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
0.0005
NADPH
Rattus norvegicus
-
pH 7.0, 25C, mutant K153M
0.0006
NADPH
Rattus norvegicus
-
pH 7.0, 25C, mutant S136A
0.0009
NADPH
Rattus norvegicus
-
pH 7.0, 25C, mutant Y149F
1.5
NADPH
Homo sapiens
-
pH 7.0, 25C
7.75
NADPH
Trichoderma reesei
G0RH19
pH 7.0, 30C, recombinant enzyme, with L-xylulose
25
NADPH
Rattus norvegicus
-
pH 7.0, 25C, wild-type enzyme
25
NADPH
Rattus norvegicus
Q920P0
pH 7.0, 25C
26
NADPH
Cavia porcellus
Q920N9
pH 7.0, 25C
27
NADPH
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
34
NADPH
Mus musculus
Q91X52
pH 7.0, 25C
0.6
xylitol
Homo sapiens
-
pH 7.0, 25C
1
xylitol
Trichoderma reesei
G0RH19
pH 7.0, 30C, recombinant enzyme
2 - 8
xylitol
Mesocricetus auratus
Q91XV4
pH 7.0, 25C
5.6
xylitol
Neurospora crassa
-
-
10
xylitol
Rattus norvegicus
Q920P0
pH 7.0, 25C
17
xylitol
Mus musculus
Q91X52
pH 7.0, 25C
20
xylitol
Cavia porcellus
Q920N9
pH 7.0, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
0.00037
4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide
-
competitive with respect to xylitol
0.00044
4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide
-
uncompetitive with respect to NADPH
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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
LITERATURE
6.5
-
reduction of L-xylulose
7
-
assay at
7
-
assay at
7
forward, reduction reaction
7
-
assay at
7
-
reductase activity
7
reduction reaction
7.5
-
approximately
9
reverse, oxidation reaction
9
-
oxidase activity
9
oxidation reaction
10 - 11
-
oxidation of xylitol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
-
reduction of L-xylulose
7 - 10.5
-
pH 7.0: about 40% of maximal activity, pH 10.5: about 60% of maximal activity, oxidase activity
8 - 11.5
-
oxidation of xylitol
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
25
-
assay at
25
assay at
25
-
assay at
37
-
reductase activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 55
-
15C: about 65% of maximal activity, 55C: about 60% of maximal activity, reductase activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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
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
-
low expression level
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
-
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
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
low expression level
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
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
102000
-
4D2P, nondenaturing PAGE
246420
136000
-
non-denaturing PAGE
285658
250000
-
gel filtration
285665
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 26500
?
-
x * 31000, SDS-PAGE
?
-
x * 31000
-
octamer
-
8 * 32000, SDS-PAGE
tetramer
-
4 * 40000, about, sequence calculation
tetramer
-
amino acid residues Trp242, Glu238, Arg203, and Cys244 are important for tetramer formation
tetramer
-
-
dimer
-
x-ray crystallography
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
-
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
LITERATURE
4
-
2C, 2 h stable
285663
9
-
room temperature, several h stable
285663
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
20 min stable
285663
additional information
-
stable at low temperatures
654438
additional information
-
dissociation into inactive dimers at low temperatures
654438
additional information
-
rapidly dissociates into the inactive dimeric form at low temperature
668392
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation during dialysis
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, Tris-HCl 20 mM, pH 7.0, at leat several weeks
-
0C, mitochondria, 0.15 M KCl- 0.01 M NaHCO3, minimum 2 days
-
2C, aqueous solution, many weeks
-
frozen, ammonium sulfate precipitate, several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
recombinant enzyme from Escherichia coli, native from liver
strain 4D2P, partial
-
recombinant enzyme from Escherichia coli, native from liver
recombinant wild-type and mutant enzymes from Escherichia coli
-
recombinant enzyme
-
partial from strain DM101
-
recombinant N-terminal His-tagged enzyme from Saccharomyces cerevisiae strain CEN.PK2-1D by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
expression in Saccharomyces cerevisiae
-
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
expressed in Saccharomyces cerevisiae
-
DNA sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli BL21 (DE3) cells
-
expression of wild-type and mutant enzymes in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
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
-
expressed in Escherichia coli as a His6 tag fusion protein
-
Tn5 transposon transfer
-
expression of wild-type and mutant enzymes in Escherichia coli
-
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
-
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae strain MA-R4
-
expressed in Saccharomyces cerevisiae strains MA-N2, MA-N3, MA-N4, and MA-N5
-
expression of Pichia stipitis mutated XYL2 (D207/I208R/F209S or XYL2 S96C/S99C/Y102C/D207A/I208R/F209S) in Saccharomyces cerevisiae
-
gene lxr3, phylogenetic analysis, cloning in Escherichia coli strain JM109, expression of N-terminal His-tagged in Saccharomyces cerevisiae strain CEN.PK2-1D
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
transcription of lxr3 is specifically induced by L-arabinose and L-arabitol
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
H146L
-
site-directed mutagenesis, altered activity
H146L
-
IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 7.8fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 6.7fold higher than wild-type value
K153M
-
site-directed mutagenesis, active site mutant, complete loss of activity
L143F
-
site-directed mutagenesis, altered activity
L143F
-
IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 8.3fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 1.9fold higher than wild-type value
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
W191F
-
site-directed mutagenesis, altered activity
W191F
-
IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 3.4fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 7.3fold higher than wild-type value
W191S
-
site-directed mutagenesis, altered activity
W191S
-
IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 13fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 1.5fold lower than wild-type value
Y149F
-
site-directed mutagenesis, active site mutant, complete loss of activity
additional information
library screening and isolation of a dhs-21 deletion mutant
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
additional information
-
several mutants per site-directed mutagenesis to change the coenzyme binding specificity, mutants showed reduced NAD+ specificity
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
deletion of gene lxr3 leads to a significant reduction in NADPH specific LXR activity after replacement to both media containing L-arabinose
additional information
-
deletion of gene lxr3 leads to a significant reduction in NADPH specific LXR activity after replacement to both media containing L-arabinose
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
enzyme is a target for design and development of potent and specific structure-based inhibitors binding in the active site