1.1.1.9: D-xylulose reductase
This is an abbreviated version!
For detailed information about D-xylulose reductase, go to the full flat file.
Word Map on EC 1.1.1.9
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1.1.1.9
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xanthine
-
xylose
-
stipitis
-
pichia
-
xylulokinase
-
uric
-
lignocellulosic
-
pentose
-
candida
-
molybdenum
-
xylose-fermenting
-
allopurinol
-
hypoxanthine
-
xanthinuria
-
xylose-utilizing
-
hydrolysate
-
l-arabitol
-
guilliermondii
-
bagasse
-
bioethanol
-
l-arabinose
-
hemicellulosic
-
marxianus
-
scheffersomyces
-
rosy
-
d-sorbitol
-
oxygen-limited
-
l-xylulose
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mocos
-
tannophilus
-
oxydans
-
ribitol
-
molecular biology
-
gluconobacter
-
pachysolen
-
pseudoobscura
-
sulfurase
-
shehatae
-
synthesis
-
biotechnology
- 1.1.1.9
- xanthine
- xylose
- stipitis
- pichia
- xylulokinase
-
uric
-
lignocellulosic
- pentose
- candida
- molybdenum
-
xylose-fermenting
- allopurinol
- hypoxanthine
-
xanthinuria
-
xylose-utilizing
- hydrolysate
- l-arabitol
- guilliermondii
- bagasse
-
bioethanol
- l-arabinose
-
hemicellulosic
- marxianus
- scheffersomyces
-
rosy
- d-sorbitol
-
oxygen-limited
- l-xylulose
- mocos
- tannophilus
- oxydans
- ribitol
- molecular biology
- gluconobacter
- pachysolen
- pseudoobscura
-
sulfurase
- shehatae
- synthesis
- biotechnology
Reaction
Synonyms
2,3-cis-polyol(DPN) dehydrogenase (C3-5), D-xylulose reductase A, erythritol dehydrogenase, GmXDH, IoXyl2p, McXDH, More, NAD+-dependent XDH, NAD+-dependent xylitol dehydrogenase, NAD+-linked xylitol dehydrogenase, NAD-dependent xylitol dehydrogenase, NADH-dependent XDH, NADH-dependent xylitol dehydrogenase, nicotinamide adenine dinucleotide-dependent xylitol dehydrogenase 2, pentitol-DPN dehydrogenase, Ps-XDH, PsXDH, reductase, D-xylulose, RpXDH, slSDH, SpXYL2.2, SsXyl2p, TdXyl2p, XDH, XDH-Y25, xdhA, XL2, XYL2, XYL2.1, XYL2.2, xylitol dehydrogenase, xylitol dehydrogenase 2, xylitol-2-dehydrogenase
ECTree
1.1.1.9 D-xylulose reductaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.1.1.9 - D-xylulose reductase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
erythritol + NAD+
? + NADH + H+
0.77% of the activity with xylitol
-
-
?
galactitol + NAD+
? + NADH + H+
0.98% of the activity with xylitol
-
-
?
L-arabinitol + NAD+
? + NADH + H+
21% of the activity with xylitol
-
-
?
D-fructose + NADH + H+
sorbitol + NAD+
-
46.4% activity compared to D-xylulose
-
-
r
D-fructose + NADH + H+
sorbitol + NAD+
-
46.4% activity compared to D-xylulose
-
-
r
D-mannitol + NAD+
?
-
16.1% activity compared to xylitol
-
-
?
D-mannitol + NAD+
?
2.6% activity compared to xylitol
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
low activity compared to xylitol
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
low activity, reaction of EC 1.1.1.67
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
low activity compared to xylitol
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
low activity, reaction of EC 1.1.1.67
-
-
r
D-ribitol + NAD+
D-ribulose + NADH
-
85% of the rate of xylitol oxidation
-
-
?
D-ribitol + NAD+
D-ribulose + NADH
-
oxidation at 11% of the rate of xylitol oxidation
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
69% of activity against D-xylitol
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
rate of xylitol oxidation at 67%
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
rate of xylitol oxidation at 95%
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
rate of xylitol oxidation at 56%
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
90% of the activity with xylitol
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
71.8% activity compared to xylitol
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
71.8% activity compared to xylitol
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
oxidation at about 45%
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
rate of xylitol oxidation at 118%
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
51.3% increased activity compared to xylitol
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
51.3% increased activity compared to xylitol
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
71.8% activity compared to xylitol
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
71.8% activity compared to xylitol
-
-
?
D-xylulose + NADH + H+
D-xylitol + NAD+
-
specific for transferring the 4-pro-R hydrogen of NADH
-
-
r
L-arabitol + NAD+
L-xylulose + NADH + H+
the enzyme also has L-arabitol dehydrogenase activity (20.1% activity compared to xylitol)
-
-
?
L-arabitol + NAD+
L-xylulose + NADH + H+
about 20% activity compared to xylitol, reaction of EC 1.1.1.12
-
-
r
L-arabitol + NAD+
L-xylulose + NADH + H+
the enzyme also has L-arabitol dehydrogenase activity (20.1% activity compared to xylitol)
-
-
?
L-arabitol + NAD+
L-xylulose + NADH + H+
about 20% activity compared to xylitol, reaction of EC 1.1.1.12
-
-
r
L-erythrulose + NADH
erythritol + NAD+
-
reduction at the same rate as D-xylulose
-
-
?
L-threitol + NAD+
? + NADH + H+
0.05% of the activity with xylitol
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
reaction of EC 1.1.1.56, ribitol 2-dehydrogenase
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
reaction of EC 1.1.1.56, ribitol 2-dehydrogenase
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
60.1% activity compared to xylitol
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
60.1% activity compared to xylitol
-
-
?
sorbitol + NAD+
D-fructose + NADH + H+
-
153.9% activity compared to xylitol
-
-
r
sorbitol + NAD+
D-fructose + NADH + H+
-
153.9% activity compared to xylitol
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
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key enzyme in D-xylose metabolism
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
preferred substrate
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
preferred substrates
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
preferred substrate
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
preferred substrates
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
100% activity
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
best substrate
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NADP+
D-xylulose + NADPH + H+
wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity
-
-
?
xylitol + NADP+
D-xylulose + NADPH + H+
very low activity with NADP+
-
-
r
xylitol + NADP+
D-xylulose + NADPH + H+
mutant enzyme D205A/I260R shows activity with NADP+
-
-
r
additional information
?
-
-
the enzyme is specific for polyols that have a hydroxyl group at the C-2 and C-3 positions in the L- and D-sides, respectively, in the Fischer projection
-
-
?
additional information
?
-
-
the enzyme is specific for polyols that have a hydroxyl group at the C-2 and C-3 positions in the L- and D-sides, respectively, in the Fischer projection
-
-
?
additional information
?
-
-
specific for transferring the 4-pro-R hydrogen of NADH
-
-
?
additional information
?
-
-
no reduction of D-ribose and D-galacturonic acid
-
-
?
additional information
?
-
-
no oxidation of threitol, xylitol, sorbitol, D-iditol
-
-
?
additional information
?
-
enzyme XDH depends exclusively on NAD+/NADH as cofactors
-
-
?
additional information
?
-
-
enzyme XDH depends exclusively on NAD+/NADH as cofactors
-
-
?
additional information
?
-
-
the enzyme shows high activity to convert D-sorbitol to D-fructose. The enzyme is highly specific toward D-sorbitol and xylitol, but shows limited activity toward D-mannitol, sorbose, and glycerol. The enzyme shows no activity when glucose, inositol, galactose, mannose, rhamnose, xylose, fructose, glucuronic acid, glucolactone, 2-oxo-L-gulonic acid (2-KLG), gluconic, propanol, isopropanol, methanol, and ethanol are used as substrates
-
-
-
additional information
?
-
enzyme XDH depends exclusively on NAD+/NADH as cofactors
-
-
?
additional information
?
-
-
the enzyme shows high activity to convert D-sorbitol to D-fructose. The enzyme is highly specific toward D-sorbitol and xylitol, but shows limited activity toward D-mannitol, sorbose, and glycerol. The enzyme shows no activity when glucose, inositol, galactose, mannose, rhamnose, xylose, fructose, glucuronic acid, glucolactone, 2-oxo-L-gulonic acid (2-KLG), gluconic, propanol, isopropanol, methanol, and ethanol are used as substrates
-
-
-
additional information
?
-
-
no oxidation of threitol, xylitol, sorbitol, D-iditol
-
-
?
additional information
?
-
-
no reduction of D-fructose, L-sorbose and D-tagatose
-
-
?
additional information
?
-
-
specific for polyols of 5 or less carbon bearing cis-hydroxy groups in C2 and C3
-
-
?
additional information
?
-
-
no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
-
-
?
additional information
?
-
no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
-
-
?
additional information
?
-
-
the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabinitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol. No activity with D-mannitol, erythritol, and D-arabinitol
-
-
?
additional information
?
-
the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabinitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol. No activity with D-mannitol, erythritol, and D-arabinitol
-
-
?
additional information
?
-
the enzyme has L-arabitol dehydrogenase (LAD, EC 1.1.1.12) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
-
-
-
additional information
?
-
-
the enzyme has L-arabitol dehydrogenase (LAD, EC 1.1.1.12) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
-
-
-
additional information
?
-
-
no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
-
-
?
additional information
?
-
no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
-
-
?
additional information
?
-
-
the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabinitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol. No activity with D-mannitol, erythritol, and D-arabinitol
-
-
?
additional information
?
-
the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabinitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol. No activity with D-mannitol, erythritol, and D-arabinitol
-
-
?
additional information
?
-
the enzyme has L-arabitol dehydrogenase (LAD, EC 1.1.1.12) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
-
-
-
additional information
?
-
-
the enzyme has L-arabitol dehydrogenase (LAD, EC 1.1.1.12) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
-
-
-
additional information
?
-
-
glucose:xylose ratio of 1:2.5 promotes a 2.7fold increase in activity when compared to a glucose:xylose ratio of 1:25
-
-
?
additional information
?
-
-
no oxidation of inositol, meso-erythritol and D-(+)-arabitol
-
-
?
additional information
?
-
the enzyme shows less than 1% activity with erythritol, galactitol, D-arabitol, L-arabitol, and glycerol, and 3.1% activity with NADP+ compared to NAD+
-
-
?
additional information
?
-
-
the enzyme shows less than 1% activity with erythritol, galactitol, D-arabitol, L-arabitol, and glycerol, and 3.1% activity with NADP+ compared to NAD+
-
-
?
additional information
?
-
the enzyme shows less than 1% activity with erythritol, galactitol, D-arabitol, L-arabitol, and glycerol, and 3.1% activity with NADP+ compared to NAD+
-
-
?
additional information
?
-
-
the enzyme shows less than 1% activity with erythritol, galactitol, D-arabitol, L-arabitol, and glycerol, and 3.1% activity with NADP+ compared to NAD+
-
-
?
additional information
?
-
-
investigation of limiting metabolic steps in the utilization of xylose by recombinant Saccharomyces cerevisiae using metabolic engineering
-
-
?
