Any feedback?
No. of entries
Information on EC 1.1.1.9 - D-xylulose reductase
for references in articles please use BRENDA:EC1.1.1.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.9 D-xylulose reductase
IUBMB Comments
Also acts as an L-erythrulose reductase.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 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
showSynonyms
xdh, xylitol dehydrogenase, ioxyl2p, psxdh, tdxyl2p, rpxdh, ssxyl2p, slsdh, mcxdh, erythritol dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-cis-polyol(DPN) dehydrogenase (C3-5)
-
-
-
-
D-xylulose reductase A
erythritol dehydrogenase
-
-
-
-
IoXyl2p
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
reductase, D-xylulose
-
-
-
-
RpXDH
SpXYL2.2
SsXyl2p
TdXyl2p
XDH
XDH-Y25
xdhA
XYL2
XYL2.1
XYL2.2
xylitol dehydrogenase
xylitol dehydrogenase 2
xylitol-2-dehydrogenase
-
-
-
-
NAD-dependent xylitol dehydrogenase
-
-
-
-
nicotinamide adenine dinucleotide-dependent xylitol dehydrogenase 2
-
-
nicotinamide adenine dinucleotide-dependent xylitol dehydrogenase 2
-
-
-
XDH
-
-
-
-
xylitol dehydrogenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
xylitol + NAD+ = D-xylulose + NADH + H+
-
-
-
-
xylitol + NAD+ = D-xylulose + NADH + H+
it is concluded that the enzyme reaction follows the mechanism where coenzyme binds first and leaves last. Therefore, dissociation of D-xylulose-NADH complex is suggested to be the rate-limiting step
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
xylitol degradation I
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming)
Also acts as an L-erythrulose reductase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9028-16-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-mannitol + NAD+
? + NADH + H+
Substrates: 8% of the activity with xylitol
Products: -
Products: -
?
erythritol + NAD+
? + NADH + H+
Substrates: 0.77% of the activity with xylitol
Products: -
Products: -
?
galactitol + NAD+
? + NADH + H+
Substrates: 0.98% of the activity with xylitol
Products: -
Products: -
?
L-arabinitol + NAD+
? + NADH + H+
Substrates: 21% of the activity with xylitol
Products: -
Products: -
?
L-arabitol + NAD+
L-xylulose + NADH + H+
Substrates: about 20% activity compared to xylitol, reaction of EC 1.1.1.12
Products: -
Products: -
r
ribitol + NAD+
? + NADH + H+
Substrates: 40% of the activity with xylitol
Products: -
Products: -
?
D-fructose + NADH + H+
sorbitol + NAD+
Substrates: 46.4% activity compared to D-xylulose
Products: -
Products: -
r
D-fructose + NADH + H+
sorbitol + NAD+
Substrates: 46.4% activity compared to D-xylulose
Products: -
Products: -
r
D-iditol + NAD+
?
-
Substrates: 11.2% of the activity with xylitol
Products: -
Products: -
?
D-iditol + NAD+
?
-
Substrates: 11.2% of the activity with xylitol
Products: -
Products: -
?
D-mannitol + NAD+
?
Substrates: 16.1% activity compared to xylitol
Products: -
Products: -
?
D-mannitol + NAD+
?
Substrates: 16.1% activity compared to xylitol
Products: -
Products: -
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
Substrates: low activity, reaction of EC 1.1.1.67
Products: -
Products: -
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
Substrates: low activity, reaction of EC 1.1.1.67
Products: -
Products: -
r
D-ribitol + NAD+
D-ribulose + NADH
-
Substrates: 85% of the rate of xylitol oxidation
Products: -
Products: -
?
D-ribitol + NAD+
D-ribulose + NADH
-
Substrates: oxidation at 11% of the rate of xylitol oxidation
Products: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: -
Products: -
Products: -
ir
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: 69% of activity against D-xylitol
Products: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: -
Products: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: rate of xylitol oxidation at 67%
Products: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: rate of xylitol oxidation at 95%
Products: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: rate of xylitol oxidation at 56%
Products: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: 90% of the activity with xylitol
Products: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: oxidation at about 45%
Products: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: rate of xylitol oxidation at 118%
Products: -
Products: -
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-sorbitol + NAD+
L-sorbose + NADH + H+
Substrates: 71.8% activity compared to xylitol
Products: -
Products: -
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
Substrates: 71.8% activity compared to xylitol
Products: -
Products: -
?
D-sorbose + NADH + H+
sorbitol + NAD+
-
Substrates: low activity
Products: -
Products: -
r
D-sorbose + NADH + H+
sorbitol + NAD+
-
Substrates: low activity
Products: -
Products: -
r
D-threitol + NAD+
?
-
Substrates: 109% of the activity with xylitol
Products: -
Products: -
?
D-threitol + NAD+
?
-
Substrates: 109% of the activity with xylitol
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
Metahyphopichia silvanorum VGI-II
-
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylulose + NAD+
xylitol + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-xylulose + NADH + H+
D-xylitol + NAD+
-
Substrates: -
Products: -
Products: -
?
D-xylulose + NADH + H+
D-xylitol + NAD+
-
Substrates: specific for transferring the 4-pro-R hydrogen of NADH
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: 100% activity
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: 100% activity
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
Products: -
r
glycerol + NAD+
glycerone + NADH + H+
-
Substrates: low activity
Products: -
Products: -
r
glycerol + NAD+
glycerone + NADH + H+
-
Substrates: low activity
Products: -
Products: -
r
L-erythrulose + NADH
erythritol + NAD+
-
Substrates: reduction at the same rate as D-xylulose
Products: -
Products: -
?
L-threitol + NAD+
? + NADH + H+
Substrates: 75% of the activity with xylitol
Products: -
Products: -
?
L-threitol + NAD+
? + NADH + H+
Substrates: 0.05% of the activity with xylitol
Products: -
Products: -
?
meso-erythritol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
r
ribitol + NAD+
D-ribulose + NADH + H+
Substrates: -
Products: -
Products: -
r
ribitol + NAD+
D-ribulose + NADH + H+
Substrates: 60.1% activity compared to xylitol
Products: -
Products: -
?
ribitol + NAD+
D-ribulose + NADH + H+
Substrates: 60.1% activity compared to xylitol
Products: -
Products: -
?
sorbitol + NAD+
D-fructose + NADH + H+
Substrates: 153.9% activity compared to xylitol
Products: -
Products: -
r
sorbitol + NAD+
D-fructose + NADH + H+
Substrates: 153.9% activity compared to xylitol
Products: -
Products: -
r
Xylitol + NAD+
?
-
Substrates: inducible pathway of xylose catabolism
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: key enzyme in D-xylose metabolism
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: 100% activity
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: 100% activity
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: preferred substrates
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: 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
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: 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
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: 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
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: best substrate
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: best substrate
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Spathaspora passalidarum UFMG-CM-Y474
-
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
L-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NADP+
D-xylulose + NADPH + H+
Substrates: wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity
Products: -
Products: -
?
xylitol + NADP+
D-xylulose + NADPH + H+
Substrates: very low activity with NADP+
Products: -
Products: -
r
xylitol + NADP+
D-xylulose + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
xylitol + NADP+
D-xylulose + NADPH + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reduction of D-ribose and D-galacturonic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of threitol, xylitol, sorbitol, D-iditol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reduction of D-ribulose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reduction of D/L-xylose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: glycerol
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme XDH depends exclusively on NAD+/NADH as cofactors
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme XDH depends exclusively on NAD+/NADH as cofactors
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme XDH depends exclusively on NAD+/NADH as cofactors
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of threitol, xylitol, sorbitol, D-iditol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reduction of D-fructose, L-sorbose and D-tagatose
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for polyols of 5 or less carbon bearing cis-hydroxy groups in C2 and C3
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
Metahyphopichia silvanorum VGI-II
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucose:xylose ratio of 1:2.5 promotes a 2.7fold increase in activity when compared to a glucose:xylose ratio of 1:25
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reduction of D/L-xylose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reduction of L-xylulose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of ribitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of inositol, meso-erythritol and D-(+)-arabitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of mannitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reduction of D/L-xylose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reduction of L-xylulose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of ribitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: investigation of limiting metabolic steps in the utilization of xylose by recombinant Saccharomyces cerevisiae using metabolic engineering
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of ribitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of mannitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reduction of D/L-xylose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reduction of L-xylulose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of ribitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for transferring the 4-pro-R hydrogen of NADH
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: 100% activity
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: 100% activity
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
Products: -
r
Xylitol + NAD+
?
-
Substrates: inducible pathway of xylose catabolism
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: key enzyme in D-xylose metabolism
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: 100% activity
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: 100% activity
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: 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
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: 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
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: 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
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Spathaspora passalidarum UFMG-CM-Y474
-
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucose:xylose ratio of 1:2.5 promotes a 2.7fold increase in activity when compared to a glucose:xylose ratio of 1:25
Products: -
Products: -
?
additional information
?
-
-
Substrates: investigation of limiting metabolic steps in the utilization of xylose by recombinant Saccharomyces cerevisiae using metabolic engineering
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
stereochemistry of hydrogen transfer from xylitol, ribitol or sorbitol to NAD+ is of the (R)- or A-type
NAD+
-
xylitol oxidation favors NAD+ over NADP+, but xylulose reduction favors NADPH over NADH
NAD+
NAD+ specificity is largely conferred by Asp38, which interacts with the hydroxyls of the adenosine ribose
NAD+
-
dependent on, the wild-type enzyme prefers NAD+, while a modified mutant enzyme is also able to utilize NADP+ in the D-xylitol oxidation reaction
NAD+
the deduced XDH gene product possesses an NAD-binding glycine-rich Rossmann fold domain [GXGXXG] present in MDR superfamily
NAD+
strictly dependent on, residues Val192, Asp212, and Lys217 are responsible for NAD+ binding. Especially, Asp212 in IoXyl2p determines the specificity for NAD+, which forms double-hydrogen bonds to the hydroxyl groups in the ribosyl moiety of NAD+
NAD+
strictly dependent on, residues Val180, Asp200, and Lys205 are responsible for NAD+ binding. Especially, Asp200 in TdXyl2p determines the specificity for NAD+, which forms double-hydrogen bonds to the hydroxyl groups in the ribosyl moiety of NAD+
NADP+
-
xylitol oxidation favors NAD+ over NADP+, but xylulose reduction favores NADPH over NADH
NADP+
wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity
NADP+
-
the wild-type enzyme prefers NAD+, while a modified mutant enzyme is also able to utilize NADP+ in the D-xylitol oxidation reaction
additional information
-
at high concentrations of xylitol 1.5% as effective as NAD+
-
additional information
-
at high concentrations of xylitol 1.5% as effective as NAD+
-
additional information
-
at high concentrations of xylitol 1.5% as effective as NAD+
-
additional information
-
no oxidation of ribitol or sorbitol with NADP+
-
additional information
activity with NADP+ is 4% of the activity with NAD+
-
additional information
-
XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity
-
additional information
NADP+ is a poor cofactor giving 3.1% activity compared to NAD+
-
additional information
-
NADP+ is a poor cofactor giving 3.1% activity compared to NAD+
-
additional information
-
the enzyme exhibits high preference for NAD+ as the cofactor, while no activity with NADP+, FAD, or pyrroloquinoline quinone is observed
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Cu2+
Mg2+
Mn2+
Zn2+
additional information
Zn2+
required, the zinc ADH signature and conserved coenzyme binding motif are observed in the amino acid sequence of McXDH at positions 65-76 and 183-188 and are completely conserved among McXDH and XDHs from other yeasts and filamentous fungi
Zn2+
1 mM, 62% of the activity with Mg2+. The deduced XDH gene product possesses the Zn2+-containing ADH signature sequence [GHE]xx[G]xxxxx[G]xx[V] and the catalytic Zn2+-binding site Cys41, His66, Glu67, and Glu152
Zn2+
required, the conserved coenzyme binding motif (GxGxxG) and zinc-ADH signature (GHExxGxxxxxGxxV) are observed in the amino acid sequence of RpXDH at position 181-186 and 70-84. The ligand binding residues for catalytic zinc (residue C46, H71, E72, and E157) and structural zinc (residue C101, C104, C107, and C115) are found in the RpXDH sequence
additional information
-
no significant effect by Ni2+, Ca2+, Fe2+, and Cr3+ at 0.5 mM. 5 mM EDTA elicits no obvious effect on NAD-dependent xylitol dehydrogenase 2, indicating that the enzyme does not require a chelator for its activity
additional information
-
no activation by Zn2+, Cu2+, Ca2+, Ni2+, Co2+, Fe2+
additional information
after incubation with ZnSO4, ZnCl2, FeCl2, and CuCl2, 40, 37, 30, and 25%, respectively, of the activity of the metal-free enzyme is restored. Poorer effects by Fe3+, Cd2+, and Ca2+, while Ni2+, Mn2+, Co2+, Mg2+, K+, and Na+ do not exert restorative effects
additional information
-
after incubation with ZnSO4, ZnCl2, FeCl2, and CuCl2, 40, 37, 30, and 25%, respectively, of the activity of the metal-free enzyme is restored. Poorer effects by Fe3+, Cd2+, and Ca2+, while Ni2+, Mn2+, Co2+, Mg2+, K+, and Na+ do not exert restorative effects
additional information
KCl has not a strong effect on the enzyme activity at 0.1-1.0
additional information
-
KCl has not a strong effect on the enzyme activity at 0.1-1.0
additional information
activity is not significantly stimulated by Ba2+, Ca2+, Fe2+, Hg2+, or K+
additional information
LiCl, NaCl, MgCl2, MgSO4, ZnCl2, ZnCl4, SnCl2, NiCl2, BaCl2, and PbCl2 do not affect the enzyme activity at 1 mM
additional information
-
LiCl, NaCl, MgCl2, MgSO4, ZnCl2, ZnCl4, SnCl2, NiCl2, BaCl2, and PbCl2 do not affect the enzyme activity at 1 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
complete inhibition, enzyme activity can be partially restored by addition of Zn2+, Ni2+, Co2+, Ag+, Fe3+, and Mn2+
EDTA
strong inhibition at 1 mM, very strong inhibition at 5-10 mM
KCl
gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M
KCl
gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M
NaCl
gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M
NaCl
gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M
Zn2+
-
exogenous Zn2+ (added as ZnSO4) in the concentration range 1-100 microM is a strong irreversible inhibitor of wild-type and mutant E154C
additional information
-
not inhibitory: MgCl2, ZnCl2, CoCl2, CuCl2 at 1 mM, EDTA at 10 mM
-
additional information
-
5 mM EDTA elicits no obvious effect on NAD-dependent xylitol dehydrogenase 2, indicating that the enzyme does not require a chelator for its activity
-
additional information
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
additional information
-
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
additional information
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
additional information
-
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
additional information
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
additional information
-
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
gradually activates the enzyme with increasing concentrations of 0.1-1.0 M
Sodium acetate
-
1 g/l in reaction medium, about 15% increase of activity
additional information
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
additional information
-
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
additional information
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
additional information
-
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
additional information
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
additional information
-
glycerol has not a strong effect on the enzyme activity at 1-10 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Acquired xanthine dehydrogenase expression shortens survival in patients with resected adenocarcinoma of lung.
Arthralgia
[Xanthinuria type 1 in a woman with arthralgias: a combined clinical and molecular genetic investigation].
Arthritis, Rheumatoid
Xanthine dehydrogenase deficiency with novel sequence variations presenting as rheumatoid arthritis in a 78-year-old patient.
Atherosclerosis
Associations of hypertension and its complications with variations in the xanthine dehydrogenase gene.
Bacterial Infections
Role of xanthine dehydrogenase and aging on the innate immune response of Drosophila.
Breast Neoplasms
Low levels of both xanthine dehydrogenase and cellular retinol binding protein are responsible for retinoic acid deficiency in malignant human mammary epithelial cells.
Breast Neoplasms
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Carcinoma
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Xanthine dehydrogenase downregulation promotes TGF? signaling and cancer stem cell-related gene expression in hepatocellular carcinoma.
Crohn Disease
Influences of XDH genotype by gene-gene interactions with SUCLA2 for thiopurine-induced leukopenia in Korean patients with Crohn's disease.
Crohn Disease
P702. Influences of XDH genotype on thiopurine-induced leukopenia in Korean patients with Crohn's disease determined by gene-gene interactions.
d-xylulose reductase deficiency
Gout, uric acid and purine metabolism in paediatric nephrology.
d-xylulose reductase deficiency
The RNAi-Mediated Silencing of Xanthine Dehydrogenase Impairs Growth and Fertility and Accelerates Leaf Senescence in Transgenic Arabidopsis Plants.
d-xylulose reductase deficiency
Xanthine dehydrogenase deficiency with novel sequence variations presenting as rheumatoid arthritis in a 78-year-old patient.
Dehydration
The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid.
Drug-Related Side Effects and Adverse Reactions
Novel pharmacogenetic markers for treatment outcome in azathioprine-treated inflammatory bowel disease.
Drug-Related Side Effects and Adverse Reactions
Polymorphism of genes involved in purine metabolism (XDH, AOX1, MOCOS) in kidney transplant recipients receiving azathioprine.
Genetic Diseases, Inborn
Assignment of human xanthine dehydrogenase gene to chromosome 2p22.
Hydrocephalus
Gene expression analysis of the development of congenital hydrocephalus in the H-Tx rat.
Hypertension
Association between Serum Urate and Risk of Hypertension in Menopausal Women with XDH Gene.
Hypertension
Association between xanthine dehydrogenase tag single nucleotide polymorphisms and essential hypertension.
Hypertension
Associations of hypertension and its complications with variations in the xanthine dehydrogenase gene.
Infections
Role of xanthine dehydrogenase and aging on the innate immune response of Drosophila.
Inflammatory Bowel Diseases
AOX1 and XDH Enzymes Genotyping and its Effect on Clinical Response to Azathioprine in Inflammatory Bowel Disease Patients Among Jordanian Population.
Leukopenia
Influences of XDH genotype by gene-gene interactions with SUCLA2 for thiopurine-induced leukopenia in Korean patients with Crohn's disease.
Leukopenia
P702. Influences of XDH genotype on thiopurine-induced leukopenia in Korean patients with Crohn's disease determined by gene-gene interactions.
Lung Injury
Abdominal paracentesis drainage protects rats against severe acute pancreatitis-associated lung injury by reducing the mobilization of intestinal XDH/XOD.
Lung Neoplasms
Acquired xanthine dehydrogenase expression shortens survival in patients with resected adenocarcinoma of lung.
Lung Neoplasms
Genomic signatures defining responsiveness to allopurinol and combination therapy for lung cancer identified by systems therapeutics analyses.
Lung Neoplasms
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Melanosis
Allopurinol-induced melanism in the tiger salamander (Ambystoma tigrinum nebulosum).
Meningioma
Lead exposure, polymorphisms in genes related to oxidative stress, and risk of adult brain tumors.
Mesothelioma
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Neoplasm Metastasis
Acquired xanthine dehydrogenase expression shortens survival in patients with resected adenocarcinoma of lung.
Neoplasms
A pan-cancer study of the transcriptional regulation of uricogenesis in human tumours: pathological and pharmacological correlates.
Neoplasms
Acquired xanthine dehydrogenase expression shortens survival in patients with resected adenocarcinoma of lung.
Neoplasms
Conversion of xanthine dehydrogenase to xanthine oxidase as a possible marker for hypoxia in tumours and normal tissues.
Neoplasms
Genomic signatures defining responsiveness to allopurinol and combination therapy for lung cancer identified by systems therapeutics analyses.
Neoplasms
Low levels of both xanthine dehydrogenase and cellular retinol binding protein are responsible for retinoic acid deficiency in malignant human mammary epithelial cells.
Neoplasms
Reductive activation of doxorubicin by xanthine dehydrogenase from EMT6 mouse mammary carcinoma tumors.
Neoplasms
Targeted knock-in mice expressing the oxidase-fixed form of xanthine oxidoreductase favor tumor growth.
Neoplasms
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Neoplasms
Xanthine dehydrogenase downregulation promotes TGF? signaling and cancer stem cell-related gene expression in hepatocellular carcinoma.
Nephrolithiasis
Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria.
Neutropenia
Pathway genes and metabolites in thiopurine therapy in Korean children with acute lymphoblastic leukaemia.
Obesity
Body mass index is independently associated with xanthine oxidase activity in overweight/obese population.
Obesity
Hepatocyte-Specific Ablation or Whole-Body Inhibition of Xanthine Oxidoreductase in Mice Corrects Obesity-Induced Systemic Hyperuricemia Without Improving Metabolic Abnormalities.
Ovarian Neoplasms
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Pancreatitis
Mobilization of xanthine oxidase from the gastrointestinal tract in acute pancreatitis.
Renal Insufficiency
A mouse model of early-onset renal failure due to a xanthine dehydrogenase nonsense mutation.
Reperfusion Injury
Mechanisms of gastrointestinal ischemia-reperfusion injury and potential therapeutic interventions: a review and its implications in the horse.
Stomach Neoplasms
Genetic variants in XDH are associated with prognosis for gastric cancer in a Chinese population.
Stomach Neoplasms
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.6
NAD+
pH 9.0, 35°C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
17.3
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S/N211R
23.5
NAD+
pH 9.0, 35°C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.04
NADP+
pH 9.0, 35°C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1.18
NADP+
pH 9.0, 35°C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.38
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S/N211R
0.638
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme D207A/I208R/F209T
0.731
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme D207A/I208R/F209Y
0.897
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme D207A/I208R/F209S
1.04
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1.18
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.38
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme D207A/I208R/F209S/N211R
4 - 5.4
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme I208R/F209S
9.56
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme S96C/S99CY102C
9.96
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme D207A/F209S
10.1
xylitol
recombinant wild-type enzyme, pH 9.0, 35°C, with NAD+
21.7
xylitol
-
wild-type XDH: kcat/Km (NAD+): 2760 l/min/mmol, kcat/Km (NADP+): 2790 l/min/mmol
22.2
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A
24.2
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R
27.4
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme N211R
29.5
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme I208R
30.3
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme S96C/S99CY102C
31.1
xylitol
-
mutant D207A/I208R/F209S: kcat/Km (NAD+): 181 l/min/mmol, kcat/Km (NADP+): 0.65 l/min/mmol
34.1
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme F209S
45.2
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/F209S
50.1
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R/F209Y
55.7
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R/F209S
97.8
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R/F209T
111
xylitol
-
mutant S96C/S99C/Y102C/D207A/I208R/F209S: kcat/Km (NADP+): 10700 l/min/mmol
additional information
additional information
-
steady-state kinetic analysis of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of mutant enzymes in engineered strains, detailed overview
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
NAD+
pH 9.0, 35°C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
13.17
NAD+
pH 9.0, 35°C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
23.83
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S/N211R
29.5
NAD+
pH 9.0, 35°C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
183.3
NADP+
pH 9.0, 35°C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
210
NADP+
pH 9.0, 35°C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
2 - 3.7
xylitol
recombinant mutant D205A/I206R, pH 9.0, 35°C, with NAD+
11.1
xylitol
recombinant wild-type enzyme, pH 9.0, 35°C, with NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.1
xylitol
recombinant wild-type enzyme, pH 9.0, 35°C, with NAD+
23.7
xylitol
recombinant mutant D205A/I206R, pH 9.0, 35°C, with NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.11
0.4
about, purified recombinant enzyme, substrates L-arabitol and NAD+, pH 7.0, 30°C
0.76
-
purified native enzyme, pH 11.0, 30°C, substrate meso-erythritol
10.71
pH 7.0, 30°C, recombinant enzyme with xylitol and NAD+ as substrates
13.29
pH 7.0, 30°C, recombinant enzyme with xylitol and NAD+ as substrates
135.2
purified recombinant His6-tagged enzyme, substrate D-sorbitol, pH 11.0, 30°C
14.2
14.66
pH 7.0, 30°C, recombinant enzyme with xylitol and NAD+ as substrates
151.4
purified recombinant His6-tagged enzyme, substrate D-fructose, pH 11.0, 30°C
2.16
-
specific activity of recombinant Saccharomyces cerevisiae strain TMB3057
2.2
-
recombinant enzyme expressed in Saccharomyces cerevisiae strain CEN.PK2-1C, substrate xylitol and NAD+, pH 9.0, 35°C
2.95
-
recombinant enzyme expressed in Saccharomyces cerevisiae strain CEN.PK2-1C, co-expressed with xylose reductase from Spathaspora arborariae, substrate xylitol and NAD+, pH 9.0, 35°C
326.3
purified recombinant His6-tagged enzyme, substrate D-xylulose, pH 11.0, 30°C
4.9
purified native enzyme, substrates L-arabitol and NAD+, pH 7.0, 30°C
87.8
purified recombinant His6-tagged enzyme, substrate xylitol, pH 11.0, 30°C
additional information
14.2
purified recombinant His6-tagged enzyme, substrate D-mannitol, pH 11.0, 30°C
14.2
purified recombinant His6-tagged enzyme, substrate xylitol, pH 7.0, 30°C
2
purified recombinant enzyme, substrates xylitol and NAD+, pH 7.0, 30°C
additional information
specific activity of wild-type and mutant enzymes
additional information
-
specific activity of wild-type and mutant enzymes
additional information
-
wild-type: NADP+-dependent activity: 0.005 U/mg, NAD+-dependent activity: 1.654 U/mg, mutant D207A/I208R/F209S: NADP+-dependent activity: 0.782 U/mg, NAD+-dependent activity: 0.271 U/mg, mutant S96C/S99C/Y102C/D207A/I208R/F209S: NADP+-dependent activity: 0.698 U/mg, NAD+-dependent activity: 0.136 U/mg
additional information
-
specific activity (U/min): 1110 (wild-type), 1440 (mutant S96C/S99C/Y102C), 1220 (mutant S96C/S99C/Y102C/P95S), 1510 (mutant S96C/S99C/Y102C/F98R), 1550 (mutant S96C/S99C/Y102C/E101F), 1360 (mutant S96C/S99C/Y102C/H112D), 1620 (mutant S96C/S99C/Y102C/F98R/E101F)
additional information
enzyme activities in different engineered Synechococcus elongatus strain PCC7942 variants, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11
7.5
8.6
9.5
11
optimum pH for the oxidation of xylitol in the presence of coenzyme NAD+
5
optimum pH for the for the reduction of D-xylulose in the presence of NADH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
5.5 - 9
over 50% of maximal activity within this range, profile overview
6 - 9
over 50% of maximal activity within this range, profile overview
6.5 - 9
over 50% of maximal activity within this range, profile overview
8.7 - 10.5
-
about 80% of maximal oxidation activity at pH 8.7 and 10.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
40
45
30
optimum temperature for the oxidation of xylitol in the presence of coenzyme NAD+
35
optimum temperature for the for the reduction of D-xylulose in the presence of NADH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
20°C: about 50% of maximal activity, 50°C: about 50% of maximal activity
20 - 55
25 - 40
the oxidation and reduction activities of the enzyme on the condition of temperatures ranging from 25°C to 40°C are over 80%
25 - 55
over 40% of maximal activity within this range, profile overview
25 - 60
over 40% of maximal activity within this range, profile overview
20 - 55
over 40% of maximal activity within this range, profile overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from an alcohol fermentation starter in Thailand
UniProt
brenda
isolated from an alcohol fermentation starter in Thailand
UniProt
brenda
Issatchenkia orientalis, a multistress-tolerant yeast
UniProt
brenda
Candida colliculosa, a multistress-tolerant yeast
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
the organism grows on rice straw hemicellulosic hydrolysate, as the only source of nutrient, optimization of culture conditions for production of xylitol from D-xylose, xylitol dehydrogenase remains constant, whereas the level of xylose reductase decreases when the initial xylose concentration is increased from 30 to 70 g/l, development of enzyme activities, overview
brenda
additional information
expression of xyl2 gene is increased during exponential growth phase and maintains in stationary phase at 96 h in the D-xylose culture
brenda
additional information
-
expression of xyl2 gene is increased during exponential growth phase and maintains in stationary phase at 96 h in the D-xylose culture
brenda
additional information
-
expression of xyl2 gene is increased during exponential growth phase and maintains in stationary phase at 96 h in the D-xylose culture
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the conserved coenzyme binding motif (GxGxxG) and zinc-ADH signature (GHExxGxxxxxGxxV) are observed in the amino acid sequence of RpXDH at position 181-186 and 70-84 and are completely conserved among RpXDH, XDHs, and SDHs from other filamentous fungi and yeasts
evolution
-
the enzyme contains a NAD(P)-binding motif and a classical active site motif belonging to the short-chain dehydrogenase family
evolution
the enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily and polyol dehydrogenase (PDH) subfamily. The enzyme contains the typical NAD+-binding motif GxGxxG of MDR family enzymes
evolution
-
the conserved coenzyme binding motif (GxGxxG) and zinc-ADH signature (GHExxGxxxxxGxxV) are observed in the amino acid sequence of RpXDH at position 181-186 and 70-84 and are completely conserved among RpXDH, XDHs, and SDHs from other filamentous fungi and yeasts
-
evolution
-
the enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily and polyol dehydrogenase (PDH) subfamily. The enzyme contains the typical NAD+-binding motif GxGxxG of MDR family enzymes
-
evolution
-
the enzyme contains a NAD(P)-binding motif and a classical active site motif belonging to the short-chain dehydrogenase family
-
malfunction
deletin of gene xdhA and gene ladA and or both lead mutants with decreased dehydrogenase activities and increased xylitol production, overview
malfunction
-
deletin of gene xdhA and gene ladA and or both lead mutants with decreased dehydrogenase activities and increased xylitol production, overview
-
metabolism
-
key enzymes for xylitol production in yeasts are xylose reductase and xylitol dehydrogenase, overview
metabolism
the redox balance between xylose reductase (XR) and xylitol dehydrogenase (XDH) is thought to be an important factor in effective xylose fermentation
metabolism
-
in order to overcome xylitol accumulation in Aspergillus carbonarius, a K274R point mutation is introduced into the xylose reductase with the aim of changing the specificity toward NADH. Fermentation with the mutant strain (grown on D-xylose as the sole carbon source) shows a 2.8fold reduction in xylitol accumulation and 4.5fold increase in citric acid production compared to the wild-type strain. The fact that the mutant strain shows decreased xylitol levels is assumed to be associated with the capability of the mutated xylose reductase to use NADH generated by the xylitol dehydrogenase XDH, thus preventing the inhibition of XDH by the high levels of NADH and ensuring the flux of D-xylose through the pathway
metabolism
-
the cofactor imbalance between the NAD(P)H-dependent wild type XR and NAD+-dependent XDH can create an intracellular redox imbalance, leading to an accumulation of NADH and a shortage of NAD+ necessary for the XDH reaction. The likely increase in intracellular xylitol concentration favors xylitol excretion, which reduces the ethanol yield by Saccharomyces cerevisiae
metabolism
xylitol dehydrogenase catalyzes the second step of D-xylose metabolism
metabolism
one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
metabolism
biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
metabolism
-
xylitol dehydrogenase catalyzes the second step of D-xylose metabolism
-
metabolism
-
one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
-
metabolism
-
biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
-
metabolism
-
in order to overcome xylitol accumulation in Aspergillus carbonarius, a K274R point mutation is introduced into the xylose reductase with the aim of changing the specificity toward NADH. Fermentation with the mutant strain (grown on D-xylose as the sole carbon source) shows a 2.8fold reduction in xylitol accumulation and 4.5fold increase in citric acid production compared to the wild-type strain. The fact that the mutant strain shows decreased xylitol levels is assumed to be associated with the capability of the mutated xylose reductase to use NADH generated by the xylitol dehydrogenase XDH, thus preventing the inhibition of XDH by the high levels of NADH and ensuring the flux of D-xylose through the pathway
-
metabolism
-
one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
-
metabolism
-
biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
-
metabolism
-
one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
-
metabolism
-
biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
-
physiological function
strictly NADPH-dependent XR with mutated strict NADP+-dependent XDH are more effective in increasing bioethanol production and decreasing xylitol accumulation than the NAD+-dependent wild-type XDH, overview
physiological function
enzyme XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity directly limiting the overall conversion process of D-xylose fermentation to ethanol by Gluconobacter oxydans
physiological function
the organism catabolizes L-arabinose as well as D-glucose and D-xylose. The highest production amounts of ethanol from D-glucose, xylitol from D-xylose, and L-arabitol from L-arabinose were 0.45 g/g D-glucose, 0.60 g/g D-xylose, and 0.61 g/g L-arabinose with 21.7 g/l ethanol, 20.2 g/l xylitol, and 30.3 g/l L-arabitol, respectively. The enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
physiological function
-
enzyme XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity directly limiting the overall conversion process of D-xylose fermentation to ethanol by Gluconobacter oxydans
-
physiological function
-
the organism catabolizes L-arabinose as well as D-glucose and D-xylose. The highest production amounts of ethanol from D-glucose, xylitol from D-xylose, and L-arabitol from L-arabinose were 0.45 g/g D-glucose, 0.60 g/g D-xylose, and 0.61 g/g L-arabinose with 21.7 g/l ethanol, 20.2 g/l xylitol, and 30.3 g/l L-arabitol, respectively. The enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
-
additional information
-
XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity limiting the the overall conversion process, improvement by recombinant expression of enzyme and glucose dehydrogenase cofactor regeneration enzyme
additional information
-
xylitol production of wild-type and mutant strains, overview
additional information
xylitol production of wild-type and mutant strains, overview
additional information
enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding
additional information
-
enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding
additional information
enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding
additional information
-
enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding
additional information
-
xylitol production of wild-type and mutant strains, overview
-
additional information
-
XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity limiting the the overall conversion process, improvement by recombinant expression of enzyme and glucose dehydrogenase cofactor regeneration enzyme
-
additional information
Pichia kudriavzevii QLB_09
-
enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding
-
additional information
Torulaspora delbrueckii BLQ_03
-
enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding
-
Show AA Sequence and Transmembrane Helices (2506 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
40000
80000
recombinant enzyme, gel filtration, non-denaturing PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homopentamer
homotetramer
tetramer
?
-
x * 36600, about, sequence calculation, x * 38000, recombinant enzyme, SDS-PAGE
?
-
x * 36600, about, sequence calculation, x * 38000, recombinant enzyme, SDS-PAGE
-
homodimer
2 * 39185, sequence calculation, 2 * 41000, native enzyme, SDS-PAGE
homodimer
-
2 * 39185, sequence calculation, 2 * 41000, native enzyme, SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of the holoenzyme to 1.9 A resolution
multi-template homology modeling. The structural model of XDH obtained consists of a classical alpha/beta Rossmann fold pattern commonly found in the MDR family, which is organized into two beta-barrel domains, the coenzyme-binding residues 163-300 and catalytic residues 1-162, 301-364
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D38S/M39R
the mutant enzyme is able to exclusively use NADP+, with no loss of activity
D205A
site-directed mutagenesis, coenzyme preference of the mutant RpXDH is partially reversed from NAD+ to NADP+
D205A/I206R
site-directed mutagenesis, coenzyme preference of the mutant RpXDH is reversed from NAD+ to NADP+
D205A
-
site-directed mutagenesis, coenzyme preference of the mutant RpXDH is partially reversed from NAD+ to NADP+
-
D205A/I206R
-
site-directed mutagenesis, coenzyme preference of the mutant RpXDH is reversed from NAD+ to NADP+
-
D207A
kcat/Km for NAD+ is 3.6fold lower than wild-type value, kcat/Km for NADP+ is 4.3fold higher than wild-type value
D207A/F209S
kcat/Km for NAD+ is 2.2fold lower than wild-type value, kcat/Km for NADP+ is 745fold higher than wild-type value
D207A/I208R
kcat/Km for NAD+ is 2.5fold lower than wild-type value, kcat/Km for NADP+ is 229fold higher than wild-type value
D207A/I208R/F209S
D207A/I208R/F209S/N211R
kcat/Km for NAD+ is 32.9fold lower than wild-type value, kcat/Km for NADP+ is 4292fold higher than wild-type value, increased thermostability
D207A/I208R/F209T
kcat/Km for NAD+ is 2.4fold lower than wild-type value, kcat/Km for NADP+ is 4754fold higher than wild-type value
D207A/I208R/F209Y
kcat/Km for NAD+ is 6.9fold lowerthan wild-type value, kcat/Km for NADP+ is 788fold higher than wild-type value
F209S
kcat/Km for NAD+ is 1.9fold lower than wild-type value, kcat/Km for NADP+ is 31.4fold higher than wild-type value
I208R
kcat/Km for NAD+ is nearly identical to wild-type value, kcat/Km for NADP+ is 44fold higher than wild-type value
I208R/F209S
kcat/Km for NAD+ is 30.7fold lower than wild-type value, kcat/Km for NADP+ is 1.5fold higher than wild-type value
N211R
kcat/Km for NAD+ is 1.1fold lower than wild-type value, kcat/Km for NADP+ is 7.6fold higher than wild-type value
S96C/S99C/Y102C
-
specific activity (U/min): 1440, half denaturation temperature T1/2 (°C): 46.1, thermal transition temperature Tcd (°C): 47.5
S96C/S99C/Y102C/D207A/I208R/F209S
S96C/S99C/Y102C/D207A/I208R/F209S/N211R
kcat/Km for NAD+ is 26.5fold lower than wild-type value, kcat/Km for NADP+ is 16154fold higher than wild-type value
S96C/S99C/Y102C/E101F
-
specific activity (U/min): 1550, half denaturation temperature T1/2 (°C): 50.9, thermal transition temperature Tcd (°C): 50.5
S96C/S99C/Y102C/F98R
-
specific activity (U/min): 1510, half denaturation temperature T1/2 (°C): 53.1, thermal transition temperature Tcd (°C): 51.7
S96C/S99C/Y102C/F98R/E101F
-
specific activity (U/min): 1620, half denaturation temperature T1/2 (°C): 56.0, thermal transition temperature Tcd (°C): 53.8
S96C/S99C/Y102C/H112D
-
specific activity (U/min): 1360, half denaturation temperature T1/2 (°C): 44.0, thermal transition temperature Tcd (°C): 47.0
S96C/S99C/Y102C/P95S
-
specific activity (U/min): 1220, half denaturation temperature T1/2 (°C): 37.4, thermal transition temperature Tcd (°C): 43.5
S96C/S99CY102C
kcat/Km for NAD+ is 1.1fold lower than wild-type value, kcat/Km for NADP+ is 8.8fold higher than wild-type value
D202A/L203R/V204S/E205P/S206R
-
site-directed mutagenesis, introduction of multiple site-directed mutations in the coenzyme-binding pocket of Galactocandida mastotermitis XDH to enable activity with NADP+, which is lacking in the wild-type enzyme, genetic metabolic engineering for improvement of xylose metabolism and fermentation in wild-type Saccharomyces cerevisiae strains, which are not able to naturally metabolize D-xylulose, overview
E154C
-
mutant bearing a disrupted Zn2+ binding site: purified preparations show a variable Zn2+ (0.10-0.40 atom/subunit), mutant exhibits a constant catalytic Zn2+ centre activity and does not require exogenous Zn2+ for activity or stability. E154C retains 0.019% and 0.74% of wild-type catalytic efficiency (kcat/Km (sorbitol): 7800/Msec and kcat:161/sec) for NAD+-dependent oxidation of sorbitol at 25°C respectively. The pH profile of kcat/Ksorbitol for E154C decreases below an apparent pK of 9.1, reflecting a shift in pK by about +1.7-1.9 pH units compared with the corresponding pH profiles for wild-type. IC50 (ZnSO4): 0.005 mM
synthesis
-
use of enzyme in a process for producing xylitol from D-glucose
additional information
D207A/I208R/F209S
kcat/Km for NAD+ is 15.2fold lower than wild-type value, kcat/Km for NADP+ is 4292fold higher than wild-type value, increased thermostability
D207A/I208R/F209S
-
mutant bearing a reversal of coenzyme specificity from NAD+ to NADP+ is introduced into Saccharomyces cerevisiae. kcat/Km (NAD+): 181 l/min/mmol, kcat/Km (NADP+): 2790 l/min/mmol, Km (xylitol in the presence of NAD+): 31.1 mM, NADP+-dependent activity: 0.782 U/mg, NAD+-dependent activity: 0.271 U/mg. In xylose fermentation a large decrease in xylitol and glycerol yield is shown, while the xylose consumption and ethanol yield are decreased
S96C/S99C/Y102C/D207A/I208R/F209S
kcat/Km for NAD+ is 36.7fold lower than wild-type value, kcat/Km for NADP+ 16462is fold higher than wild-type value
S96C/S99C/Y102C/D207A/I208R/F209S
-
mutant bearing a reversal of coenzyme specificity from NAD+ to NADP+ and additional zinc-binding site for thermostability, is introduced into Saccharomyces cerevisiae. kcat/Km (NADP+): 10700 l/min/mmol, Km (xylitol in the presence of NAD+): 111 mM , NADP+-dependent activity: 0.689 U/mg, NAD+-dependent activity: 0.136 U/mg. The xylose consumption and ethanol yield are decreased, and the xylitol yield is increased, because of low XDH activity
additional information
-
generation of xdhA and ladA deletion mutants and double-deletion mutant, that show decreased dehydrogenase activities and increased xylitol production from D-xylose compared to the KBN616 wild-type strain, overview
additional information
generation of xdhA and ladA deletion mutants and double-deletion mutant, that show decreased dehydrogenase activities and increased xylitol production from D-xylose compared to the KBN616 wild-type strain, overview
additional information
-
construction of deletion mutants of xdhA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
additional information
construction of deletion mutants of xdhA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
additional information
construction of xdhA gene disruption mutant xdhA2-1 by homologous transformation into Aspergillus oryzae strain P5 (DELTApyrG), and pyrG is used as a selectable marker, phenotype, overview
additional information
-
construction of xdhA gene disruption mutant xdhA2-1 by homologous transformation into Aspergillus oryzae strain P5 (DELTApyrG), and pyrG is used as a selectable marker, phenotype, overview
additional information
-
generation of xdhA and ladA deletion mutants and double-deletion mutant, that show decreased dehydrogenase activities and increased xylitol production from D-xylose compared to the KBN616 wild-type strain, overview
-
additional information
-
construction of deletion mutants of xdhA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
-
additional information
-
construction of xdhA gene disruption mutant xdhA2-1 by homologous transformation into Aspergillus oryzae strain P5 (DELTApyrG), and pyrG is used as a selectable marker, phenotype, overview
-
additional information
-
strain overexpressing enzyme has improved xylitol productivity, production of up to 57g/l xylitol from 225 g/l D-arabitol, via D-xylulose
additional information
-
to improve characteristics of xylose fermentation, the recombinant strain Delta xyl1 Delta xyl2-ADelta xyl2-B, with deletions of genes encoding first enzymes of xylose utilization (NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases, respectively), is constructed and used as a recipient for co-overexpression of the Escherichia coli xylA gene coding for xylose isomerase and endogenous XYL3 gene coding for xylulokinase. Recombinant strains display improved ethanol production during the fermentation of xylose
additional information
-
recombinant Saccharomyces cerevisiae strain TMB3057 with high activity of both xylose reductase and xylitol dehydrogenase show increased ethanol formation from xylose at the expense of xylitol formation
additional information
-
coenzyme specificities of the NADPH-preferring xylose reductase, EC 1.1.1.307, and the NAD+-dependent xylitol dehydrogenase are targeted in previous studies by protein design or evolution with the aim of improving the recycling of NADH or NADPH in their two-step pathway, converting xylose to xylulose. Yeast strains expressing variant pairs of both enzymes that according to in vitro kinetic data are suggested to be much better matched in coenzyme usage than the corresponding pair of wild-type enzymes, exhibit widely varying capabilities for xylose fermentation, bi-substrate kinetic analysis, and statistical analysis, overview. Engineered strains of Saccharomyces cerevisiae have engineered forms of xylose reductase or xylose dehydrogenase and imporved performance in xylose fermentation
additional information
Saccharomyces cerevisiae, the preferred microorganism for large-scale ethanol production, does not naturally consume xylose. Xylose isomerase (XI) and xylose reductase/xylitol dehydrogenase (XR/XDH) pathways are introduced into two robust industrial Saccharomyces cerevisiae strains, PE-2DELTAGRE3 and CA11, evaluated in synthetic media and corn cob hemicellulosic hydrolysate (non-detoxified corn cob hydrolysate) and the results are correlated with the differential enzyme activities found in the xylose-pathway engineered strains, evaluation of xylose fermentation capacity in oxygen-deprived conditions at 30°C and 40°C. Regarding the CA11-derived strains, the XR activity is higher in the strain with both pathways than in the one solely expressing XR/XDH, while the XDH activity at 30°C is higher in the CA11-XR/XDH strain. The sole expression of XI increases the fermentative capacity of both strains in synthetic media at 30°C and 40°C: decreasing xylitol accumulation and improving xylose consumption and ethanol production. Similar results are observed in fermentations of detoxified hydrolysate. However, in the presence of lignocellulosic-derived inhibitors, a positive synergistic effect results from the expression of both XI and XR/XDH, possibly caused by a cofactor equilibrium between the XDH and furan detoxifying enzymes, increasing the ethanol yield by more than 38%. Advantage of using the XI from Clostridium phytofermentans to attain high ethanol productivities and yields from xylose, and the simultaneous utilization of XR/XDH and XI pathways compared to the single expression of XR/XDH or XI improves ethanol production from non-detoxified hemicellulosic hydrolysates
additional information
-
Saccharomyces cerevisiae, the preferred microorganism for large-scale ethanol production, does not naturally consume xylose. Xylose isomerase (XI) and xylose reductase/xylitol dehydrogenase (XR/XDH) pathways are introduced into two robust industrial Saccharomyces cerevisiae strains, PE-2DELTAGRE3 and CA11, evaluated in synthetic media and corn cob hemicellulosic hydrolysate (non-detoxified corn cob hydrolysate) and the results are correlated with the differential enzyme activities found in the xylose-pathway engineered strains, evaluation of xylose fermentation capacity in oxygen-deprived conditions at 30°C and 40°C. Regarding the CA11-derived strains, the XR activity is higher in the strain with both pathways than in the one solely expressing XR/XDH, while the XDH activity at 30°C is higher in the CA11-XR/XDH strain. The sole expression of XI increases the fermentative capacity of both strains in synthetic media at 30°C and 40°C: decreasing xylitol accumulation and improving xylose consumption and ethanol production. Similar results are observed in fermentations of detoxified hydrolysate. However, in the presence of lignocellulosic-derived inhibitors, a positive synergistic effect results from the expression of both XI and XR/XDH, possibly caused by a cofactor equilibrium between the XDH and furan detoxifying enzymes, increasing the ethanol yield by more than 38%. Advantage of using the XI from Clostridium phytofermentans to attain high ethanol productivities and yields from xylose, and the simultaneous utilization of XR/XDH and XI pathways compared to the single expression of XR/XDH or XI improves ethanol production from non-detoxified hemicellulosic hydrolysates
additional information
-
Saccharomyces cerevisiae, the preferred microorganism for large-scale ethanol production, does not naturally consume xylose. Xylose isomerase (XI) and xylose reductase/xylitol dehydrogenase (XR/XDH) pathways are introduced into two robust industrial Saccharomyces cerevisiae strains, PE-2DELTAGRE3 and CA11, evaluated in synthetic media and corn cob hemicellulosic hydrolysate (non-detoxified corn cob hydrolysate) and the results are correlated with the differential enzyme activities found in the xylose-pathway engineered strains, evaluation of xylose fermentation capacity in oxygen-deprived conditions at 30°C and 40°C. Regarding the CA11-derived strains, the XR activity is higher in the strain with both pathways than in the one solely expressing XR/XDH, while the XDH activity at 30°C is higher in the CA11-XR/XDH strain. The sole expression of XI increases the fermentative capacity of both strains in synthetic media at 30°C and 40°C: decreasing xylitol accumulation and improving xylose consumption and ethanol production. Similar results are observed in fermentations of detoxified hydrolysate. However, in the presence of lignocellulosic-derived inhibitors, a positive synergistic effect results from the expression of both XI and XR/XDH, possibly caused by a cofactor equilibrium between the XDH and furan detoxifying enzymes, increasing the ethanol yield by more than 38%. Advantage of using the XI from Clostridium phytofermentans to attain high ethanol productivities and yields from xylose, and the simultaneous utilization of XR/XDH and XI pathways compared to the single expression of XR/XDH or XI improves ethanol production from non-detoxified hemicellulosic hydrolysates
-
additional information
-
expression of the xylitol dehydrogenase-encoding gene XYL2 of Pichia stipitis in the transketolase-deficient Saccharomyces cerevisiae strain results in an 8.5fold enhancement of the total amount of the excreted sugar alcohols ribitol and xylitol. The additional introduction of the 2-deoxy-glucose 6-phosphate phosphatase-encoding gene DOG1 into the transketolase-deficient strain expressing the XYL2 gene resulted in a further 1.6fold increase in ribitol production
additional information
engineered Saccharomyces cerevisiae strain DGX23 overexpressing aldose reductase GRE3, xylitol dehydrogenase XYL2, and xylulokinase XYL3 can ferment xylose as well as a mixture of glucose and xylose with higher ethanol yields and productivities than those of an isogenic strain overexpressing xylose reductase XYL1, xylitol dehydrogenase XYL2, and xylulokinase XYL3 under oxygen-limited conditions. Optimized expression levels of GRE3, XYL2, and XYL3 can overcome redox imbalance during xylose fermentation by engineered Saccharomyces cerevisiae under oxygen-limited conditions, anaerobic xylose fermentation
additional information
-
engineered Saccharomyces cerevisiae strain DGX23 overexpressing aldose reductase GRE3, xylitol dehydrogenase XYL2, and xylulokinase XYL3 can ferment xylose as well as a mixture of glucose and xylose with higher ethanol yields and productivities than those of an isogenic strain overexpressing xylose reductase XYL1, xylitol dehydrogenase XYL2, and xylulokinase XYL3 under oxygen-limited conditions. Optimized expression levels of GRE3, XYL2, and XYL3 can overcome redox imbalance during xylose fermentation by engineered Saccharomyces cerevisiae under oxygen-limited conditions, anaerobic xylose fermentation
additional information
enzyme XDH is changed from NAD+-dependent to NADP+-dependent, xylitol accumulation is reduced and ethanol production improved using protein engineering for reversing the dependency of XDH from NAD+ to NADP+. Construction of a set of recombinant Saccharomyces cerevisiae carrying a mutated strictly NADPH-dependent XR and NADP+-dependent XDH genes with overexpression of endogenous xylulokinase (XK), effects of complete NADPH/NADP+ recycling on ethanol fermentation and xylitol accumulation, overview. The mutated strains demonstrate 0% and 10% improvement in ethanol production, and reduced xylitol accumulation, ranging 34.4-54.7% compared with the control strain
additional information
-
enzyme XDH is changed from NAD+-dependent to NADP+-dependent, xylitol accumulation is reduced and ethanol production improved using protein engineering for reversing the dependency of XDH from NAD+ to NADP+. Construction of a set of recombinant Saccharomyces cerevisiae carrying a mutated strictly NADPH-dependent XR and NADP+-dependent XDH genes with overexpression of endogenous xylulokinase (XK), effects of complete NADPH/NADP+ recycling on ethanol fermentation and xylitol accumulation, overview. The mutated strains demonstrate 0% and 10% improvement in ethanol production, and reduced xylitol accumulation, ranging 34.4-54.7% compared with the control strain
additional information
engineered Sacchyromyces cerevisiae expressing NADPH-linked xylose reductase (XR) and NAD+-linked xylitol dehydrogenase (XDH) produces substantial amounts of the reduced byproducts under anaerobic conditions due to the cofactor difference of XR and XDH. While the additional expression of a water-forming NADH oxidase (NoxE) from Lactococcus lactis in engineered Saccharomyces cerevisiae with the XR/XDH pathway leads to reduced glycerol and xylitol production and increased ethanol yields from xylose, volumetric ethanol productivities by the engineered yeast decrease because of growth defects from the overexpression of noxE. High cell density inoculum for xylose fermentation by strain SR8 expressing noxE, resulting in strain SR8N, shows a higher ethanol yield and lower byproduct yields, and also exhibits a high ethanol productivity during xylose fermentation. Growth defects from noxE overexpression can be overcome in the case of fermenting lignocellulose-derived sugars such as glucose and xylosen
additional information
construction of efficient xylose-fermenting Saccharomyces cerevisiae strain DXS through a synthetic isozyme system of xylose reductase from Scheffersomyces stipitis. The xylose-metabolic genes XYL1 (EC 1.1.1.307), XYL2, and XYL3 (EC 2.7.1.17) from Scheffersomyces stipitis are introduced into Saccharomyces cerevisiae. Construction of control strains SR6 and MM through random integration of the XR (NADPH) or mXR (NADH) expression cassette, respectively, at the multipled elements of the genome of Saccharomyces cerevisiae strain D452-2. Fermentation parameters of engineered Saccharomyces cerevisiae strains in mixed sugar fermentations (glucose and xylose), overview
additional information
efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview
additional information
-
engineered Sacchyromyces cerevisiae expressing NADPH-linked xylose reductase (XR) and NAD+-linked xylitol dehydrogenase (XDH) produces substantial amounts of the reduced byproducts under anaerobic conditions due to the cofactor difference of XR and XDH. While the additional expression of a water-forming NADH oxidase (NoxE) from Lactococcus lactis in engineered Saccharomyces cerevisiae with the XR/XDH pathway leads to reduced glycerol and xylitol production and increased ethanol yields from xylose, volumetric ethanol productivities by the engineered yeast decrease because of growth defects from the overexpression of noxE. High cell density inoculum for xylose fermentation by strain SR8 expressing noxE, resulting in strain SR8N, shows a higher ethanol yield and lower byproduct yields, and also exhibits a high ethanol productivity during xylose fermentation. Growth defects from noxE overexpression can be overcome in the case of fermenting lignocellulose-derived sugars such as glucose and xylosen
-
additional information
-
construction of efficient xylose-fermenting Saccharomyces cerevisiae strain DXS through a synthetic isozyme system of xylose reductase from Scheffersomyces stipitis. The xylose-metabolic genes XYL1 (EC 1.1.1.307), XYL2, and XYL3 (EC 2.7.1.17) from Scheffersomyces stipitis are introduced into Saccharomyces cerevisiae. Construction of control strains SR6 and MM through random integration of the XR (NADPH) or mXR (NADH) expression cassette, respectively, at the multipled elements of the genome of Saccharomyces cerevisiae strain D452-2. Fermentation parameters of engineered Saccharomyces cerevisiae strains in mixed sugar fermentations (glucose and xylose), overview
-
additional information
-
efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview
-
additional information
-
construction of efficient xylose-fermenting Saccharomyces cerevisiae strain DXS through a synthetic isozyme system of xylose reductase from Scheffersomyces stipitis. The xylose-metabolic genes XYL1 (EC 1.1.1.307), XYL2, and XYL3 (EC 2.7.1.17) from Scheffersomyces stipitis are introduced into Saccharomyces cerevisiae. Construction of control strains SR6 and MM through random integration of the XR (NADPH) or mXR (NADH) expression cassette, respectively, at the multipled elements of the genome of Saccharomyces cerevisiae strain D452-2. Fermentation parameters of engineered Saccharomyces cerevisiae strains in mixed sugar fermentations (glucose and xylose), overview
-
additional information
-
efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview
-
additional information
-
construction of efficient xylose-fermenting Saccharomyces cerevisiae strain DXS through a synthetic isozyme system of xylose reductase from Scheffersomyces stipitis. The xylose-metabolic genes XYL1 (EC 1.1.1.307), XYL2, and XYL3 (EC 2.7.1.17) from Scheffersomyces stipitis are introduced into Saccharomyces cerevisiae. Construction of control strains SR6 and MM through random integration of the XR (NADPH) or mXR (NADH) expression cassette, respectively, at the multipled elements of the genome of Saccharomyces cerevisiae strain D452-2. Fermentation parameters of engineered Saccharomyces cerevisiae strains in mixed sugar fermentations (glucose and xylose), overview
-
additional information
-
efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview
-
additional information
the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
additional information
the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
additional information
-
the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
additional information
-
combination of xylose reductase from Spathaspora arborariae with xylitol dehydrogenase from Spathaspora passalidarum to promote xylose consumption and fermentation into xylitol in Saccharomyces cerevisiae. Recombinant co-expression of Spathaspora arborariae xylose reductase gene (SaXYL1) that accepts both NADH and NADPH as co-substrates, and of Spathaspora passalidarum strain UFMG-HM.19.1AT NADPH-dependent xylose reductase (SpXYL1.1 gene) or the SpXYL2.2 gene from Spathaspora passalidarum strain UFMG-CM-Y474 in a Saccharomyces cerevisiae strain overexpressing the native XKS1 gene encoding xylulokinase, as well as being deleted in the alkaline phosphatase encoded by the PHO13 gene. Strains expressing the Spathaspora enzymes consumes xylose with xylitol as the major fermentation product. Higher specific growth rates, xylose consumption, and xylitol volumetric productivities are obtained by the co-expression of the SaXYL1 and SpXYL2.2 genes, when compared with the co-expression of the NADPH-dependent SpXYL1.1 xylose reductase. During glucose-xylose co-fermentation by the strain with co-expression of the SaXYL1 and SpXYL2.2 genes, both ethanol and xylitol are produced efficiently. Method development and evaluation, detailed overview
additional information
-
the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
-
additional information
-
the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
-
additional information
Spathaspora passalidarum UFMG-CM-Y474
-
combination of xylose reductase from Spathaspora arborariae with xylitol dehydrogenase from Spathaspora passalidarum to promote xylose consumption and fermentation into xylitol in Saccharomyces cerevisiae. Recombinant co-expression of Spathaspora arborariae xylose reductase gene (SaXYL1) that accepts both NADH and NADPH as co-substrates, and of Spathaspora passalidarum strain UFMG-HM.19.1AT NADPH-dependent xylose reductase (SpXYL1.1 gene) or the SpXYL2.2 gene from Spathaspora passalidarum strain UFMG-CM-Y474 in a Saccharomyces cerevisiae strain overexpressing the native XKS1 gene encoding xylulokinase, as well as being deleted in the alkaline phosphatase encoded by the PHO13 gene. Strains expressing the Spathaspora enzymes consumes xylose with xylitol as the major fermentation product. Higher specific growth rates, xylose consumption, and xylitol volumetric productivities are obtained by the co-expression of the SaXYL1 and SpXYL2.2 genes, when compared with the co-expression of the NADPH-dependent SpXYL1.1 xylose reductase. During glucose-xylose co-fermentation by the strain with co-expression of the SaXYL1 and SpXYL2.2 genes, both ethanol and xylitol are produced efficiently. Method development and evaluation, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 60
the enzyme partially loses its activity at 45-55°C and completely loses activity at temperatures greater than 60°C. McXDH exhibits activities of approximately 81% and 51% at 30°C and 35°C after 30 min incubation
50
60
additional information
-
wild-type: half denaturation temperature T1/2 (°C): 35.2, thermal transition temperature Tcd (°C): 43.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing/thawing inactivates, 8 cycles lead to 89% loss of activity and 11 cycles to complete inactivation
freezing/thawing inactivates, 8 cycles lead to 89% loss of activity and 11 cycles to complete inactivation
-
freezing/thawing inactivates, 8 cycles lead to 89% loss of activity and 11 cycles to complete inactivation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 469fold from sstrain NH-10 by ammonium sulfate fractionation, two different steps of anion exchange chromatography, and gel filtration
-
native enzyme by dialysis, anion exchange chromatography, ammoniuim sulfate fractionation, hydrophobic interaction chromatography, again dialysis and another different step off anion exchange chromatography, dialysis, and gel filtration, followed by repeating the last anion exchange chromatographic step. Recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and anion exchange chromatography
native enzyme from Rhizomucor pusillus strain NBRC 4578 by anion exchange chromatography, ammonium sulfate fractionation, and hydrophobic interaction chromatography, followed by ultrafiltration, and a another different step of anion exchange chromatography, ultrafiltration, and gel filtration. Next purification steps are Reactive Red 120 affinity chromatography, dialysis, and ultrafiltration. Recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Ni-NTA column chromatography and Sephacryl S-300 gel filtration
optimized extraction by cetyl trimethyl ammonium bromide reversed micelles
-
partial
recombinant enzyme
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatograpphy and dialysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in transketolase-deficient Saccharomyces cerevisiae strain (W303/tkl1 tkl2/2C)
-
expression in Escherichia coli
expression of the engineered D202A/L203R/V204S/E205P/S206R mutant enzyme fron Galactocandida mastotermitis with altered cofactor specificity, co-expression with a mutant NADPH-specific xylulose reductase from Candida tenuis in Saccharomyces cerevisiae, the transformed strain shows up to 50% decreased glycerol yield without increase in ethanol during xylose fermentation, overview
-
gene SpXYL2.2, recombinant expression of the enzyme in Saccharomyces cerevisiae strain CEN.PK2-1C (MATa leu2-3112 ura3-52 trp1-289 his3-DELTA1 MAL2-8c SUC2), subcloning in Escherichia coli strain DH5alpha, co-expression with xylose reductase from Spathaspora arborariae
-
gene xdhA, coexpression of gene xdhA and cofactor regeneration enzyme, i.e. glucose dehydrogenase gene gdh from Bacillus subtilis, in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
-
gene Xyl2, DNA and amino acid sequence determination and analysis, sequence comparisons
gene xyl2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene xyl2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene xyl2, overexpression in Gluconobacter strain PXPG, coexpression with the glucose dehydrogenase gene from Bacillus subtilis
gene XYL2, recombinant expression in Saccharomyces cerevisiae strain SCB7 resulting in strains SCF202 and SCF201, coexpression of XYL2 with XYL1, encoding a xylose reductase, and the endogenous XKS1, encoding a xylulokinase, all under the control of the TDH3 promoter in the chromosomal DNA, the recombinant strain efficiently grows in minimal medium containing xylose as the sole carbon source. An additional mutations of MTH1, encoding the endogenous negative regulator of the glucose-sensing signal transduction pathway, MTH1e32, and GRR1, encoding endogenous Grr1, an Fbox protein component of an SCF ubiquitineligase complex grr1e33, enable efficient growth in medium containing high xylose concentrations, subcloning in Escherichia coli strain DH10B
-
gene xyl2, recombinant expression of the enzyme in Synechococcus elongatus strain PCC7942, functional co-expression with a xylose transporter from Escherichia coli, Ec-XylE
gene xyl2, the xylose-metabolic gene XYL2 from Scheffersomyces stipitis is introduced into Saccharomyces cerevisiae
gene XYL2.1, recombinant expression in Aureobasidium pullulans strain CBS 110374
genes XYL2 (D207A/I208R/F209S) and XYL2 (S96C/S99C/Y102C/D207A/I208R/F209S) are introduced into Saccharomyces cerevisiae, which already contain the Pichia stipitis XYL1 gene (encoding xylose reductase) and the endogenously overexpressed XKS1 gene (encoding xylulokinase)
-
overexpression of the enzyme in Saccharomyces cerevisiae strain CEN.PK 113-7D under control of the constitutive TDH3 promoter, co-expression with xylose reductase from Candida tenuis
-
recombinant enzyme expression in Saccharomyces cerevisiae strain CA11 (isolated from Brazilian Cachaca fermentation processes) and in strain PE-2DELTAGRE3 (isolated from Brazilian first generation bioethanol plants), coepxression with xylose reductase (XR)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
recombinant overexpression in Saccharomyces cerevisiae strain D452-2, coexpression with Saccharomyces cerevisiae enzymes/genes xylulokinase XKS1, and xylose reductase XYL1 or XYL3, aldose reductase GRE3. Xylose fermentation efficiency of a strain overexpressing GRE3 is dramatically increased by high expression levels of XYL2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
D-xylose induces the enzyme expression leading to accumulation of xylitol
the engineered Gluconobacter oxydans strain PXPG is constructed to coexpress the endogenous XDH gene and the cofactor regeneration glucose dehydrogenase gene from Bacillus subtilis. Activities for both enzymes are more than twofold higher in the Gluconobacter oxydans PXPG than in the wild-type strain. Increasing the XDH activity and the cofactor NADH supply improves the xylitol productivity
D-xylose induces the enzyme expression leading to accumulation of xylitol
D-xylose induces the enzyme expression leading to accumulation of xylitol
-
-
the engineered Gluconobacter oxydans strain PXPG is constructed to coexpress the endogenous XDH gene and the cofactor regeneration glucose dehydrogenase gene from Bacillus subtilis. Activities for both enzymes are more than twofold higher in the Gluconobacter oxydans PXPG than in the wild-type strain. Increasing the XDH activity and the cofactor NADH supply improves the xylitol productivity
the engineered Gluconobacter oxydans strain PXPG is constructed to coexpress the endogenous XDH gene and the cofactor regeneration glucose dehydrogenase gene from Bacillus subtilis. Activities for both enzymes are more than twofold higher in the Gluconobacter oxydans PXPG than in the wild-type strain. Increasing the XDH activity and the cofactor NADH supply improves the xylitol productivity
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
molecular biology
-
a high thermostability of PsXDH is obtained by subsequent site-directed mutagenesis of the structural zinc-binding loop. The best mutant in this study (C4/F98R/E101F) shows a 10.8 °C higher thermal transition temperature and 20.8 °C higher half denaturation temperature (T1/2) compared with wild-type
synthesis
biotechnology
-
strain overexpressing enzyme has improved xylitol productivity, production of up to 57g/l xylitol from 225 g/l D-arabitol, via D-xylulose
biotechnology
-
pretreatment of sugarcane bagasse hydrolysate to eliminate toxic compounds unsuitable for use as growth medium in xylitol production. Optimization of adsorption time, type of acid used, concentration and charcoal leads to a high ratio of xylose reductase, EC1.1.1.21, to xylitol dehydrogenase, EC1.1.1.9, of 4.5
biotechnology
-
the productivity and yield of xylitol fermentation by the XYL2-disrupted mutant are remarkably enhanced by screening suitable cosubstrates and optimizing the process
biotechnology
-
cells previously grown in sugar cane bagasse hemicellulosic hydrolysate are effective in enhancing xylitol production by keeping the xylose reductase (EC 1.1.1.21) activity at high levels, reducing the xylitol dehydrogenase (EC 1.1.1.9) activity and increasing xylitol volumetric productivity (26.5%) with respect to the inoculum cultivated in semidefined medium.Therefore, inoculum adaptation to sugar cane bagasse hemicellulosic hydrolysate is an important strategy to improve xylitol productivity
synthesis
-
optimization of xylitol production, using fed-batch process and controlled pH 6.0 gives maximum enzyme activity
synthesis
-
use of enzyme in xylose fermentation, metabolic flux partitioning from xylitol to xylulose depends on aeration and enzyme activity, increased aeration results in less xylitol accumulation and more xylulose accumulation, increase in enzyme activity can reduce xylitol formation
synthesis
-
use of enzyme in production of xylitol from bagasse hydrolysate, enzyme activity is higher in medium containing acetic acid than in control medium
synthesis
-
the enzyme is useful for xylitol bioproduction, profiles, overview
synthesis
-
Gluconobacter oxydans strain NH-10 is useful for production of xylitol from D-arabitol via D-xylulose
synthesis
enzyme IoXyl2p from Issatchenkia orientalis is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate
synthesis
enzyme TdXyl2p from Torulaspora delbrueckii is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate
synthesis
-
the enzyme is useful for xylitol bioproduction, profiles, overview
-
synthesis
-
the enzyme is useful for xylitol bioproduction, profiles, overview
-
synthesis
-
Gluconobacter oxydans strain NH-10 is useful for production of xylitol from D-arabitol via D-xylulose
-
synthesis
Pichia kudriavzevii QLB_09
-
enzyme IoXyl2p from Issatchenkia orientalis is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate
-
synthesis
Torulaspora delbrueckii BLQ_03
-
enzyme TdXyl2p from Torulaspora delbrueckii is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hickman, J.; Ashwell, G.
A sensitive and stereospecific enzymatic assay for xylulose
J. Biol. Chem.
234
758-761
1959
Cavia porcellus
brenda
Jakoby, W.B.; Fredericks, J.
Erythritol dehydrogenase from Aerobacter aerogenes
Biochim. Biophys. Acta
48
26-32
1961
Klebsiella aerogenes
brenda
Chiang, C.; Knight, S.G.
A new pathway of pentose metabolism
Biochem. Biophys. Res. Commun.
3
554-559
1960
Penicillium chrysogenum
brenda
Yang, V.W.; Jeffries, T.W.
Purification and properties of xylitol dehydrogenase from the xylose-fermenting yeast Candida shehatae
Appl. Biochem. Biotechnol.
26
197-206
1990
Scheffersomyces shehatae
-
brenda
Bolen, P.L.; Roth, K.A.; Freer, S.N.
Affinity purifications of aldose reductase and xylitol dehydrogenase from the xylose-fermenting yeast Pachysolen tannophilus
Appl. Environ. Microbiol.
52
660-664
1986
Pachysolen tannophilus
brenda
Alizade, M.A.; Brendel, K.; Gaede, K.
Chirality of xylitol-oxidizing enzymes from mammalian liver
FEBS Lett.
67
41-44
1976
Cavia porcellus
brenda
Doten, R.C.; Mortlock, R.P.
Inducible xylitol dehydrogenases in enteric bacteria
J. Bacteriol.
162
845-848
1985
Morganella morganii, Providencia stuartii, Serratia marcescens
brenda
Morimoto, S.; Matsuo, M.; Azuma, K.; Sinskey, A.J.
Purification and properties of D-xylulose reductase from Pachysolen tannophilus
J. Ferment. Technol.
64
219-225
1986
Pachysolen tannophilus
-
brenda
Persson, B.; Hallborn, J.; Walfridsson, M.; Hahn-Haegerdal, B.; Keraenen, S.; Penttilae, M.; Joernvall, H.
Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types
FEBS Lett.
324
9-14
1993
Scheffersomyces stipitis
brenda
Ikeuchi, T.; Kiritani, R.; Azuma, M.; Ooshima, H.
Effect of D-glucose on induction of xylose reductase and xylitol dehydrogenase in Candida tropicalis in the presence of NaCl
J. Basic Microbiol.
40
167-175
2000
Candida tropicalis
brenda
Kern, M.; Haltrich, D.; Nidetzky, B.; Kulbe, K.D.
Induction of aldose reductase and xylitol dehydrogenase activities in Candida tenuis CBS 4435
FEMS Microbiol. Lett.
149
31-37
1997
Yamadazyma tenuis, Yamadazyma tenuis CBS 4435
brenda
Singh, A.; Schuegerl, K.
Induction and regulation of D-xylose catabolizing enzymes in Fusarium oxysporum
Biochem. Int.
28
481-488
1992
Fusarium oxysporum
brenda
Takamizawa, K.; Uchida, S.; Hatsu, M.; Suzuki, T.; Kawai, K.
Development of a xylitol biosensor composed of xylitol dehydrogenase and diaphorase
Can. J. Microbiol.
46
350-357
2000
Candida tropicalis
brenda
Palnitkar, S.; Lachke, A.
Effect of nitrogen sources on oxidoreductive enzymes and ethanol production during D-xylose fermentation by Candida shehatae
Can. J. Microbiol.
38
258-260
1992
Scheffersomyces shehatae
brenda
Richard, P.; Toivari, M.H.; Penttilae, M.
Evidence that the gene YLR070c of Saccharomyces cerevisiae encodes a xylitol dehydrogenase
FEBS Lett.
457
135-138
1999
Saccharomyces cerevisiae
brenda
Jin, Y.S.; Jeffries, T.W.
Changing flux of xylose metabolites by altering expression of xylose reductase and xylitol dehydrogenase in recombinant Saccharomyces cerevisiae
Appl. Biochem. Biotechnol.
105 -108
277-286
2003
Scheffersomyces stipitis
brenda
Alves, L.A.; Vitolo, M.; Felipe, M.G.; de Almeida e Silva, J.B.
Xylose reductase and xylitol dehydrogenase activities of Candida guilliermondii as a function of different treatments of sugarcane bagasse hemicellulosic hydrolysate employing experimental design
Appl. Biochem. Biotechnol.
98-100
403-413
2002
Meyerozyma guilliermondii
brenda
Mayer, G.; Kulbe, K.D.; Nidetzky, B.
Utilization of xylitol dehydrogenase in a combined microbial/enzymatic process for production of xylitol from D-glucose
Appl. Biochem. Biotechnol.
98-100
577-589
2002
[Candida] sp. HA 167
brenda
Lima, L.H.; das Gracas de Almeida Felipe, M.; Vitolo, M.; Torres, F.A.
Effect of acetic acid present in bagasse hydrolysate on the activities of xylose reductase and xylitol dehydrogenase in Candida guilliermondii
Appl. Microbiol. Biotechnol.
65
734-738
2004
Meyerozyma guilliermondii
brenda
Sugiyama, M.; Suzuki, S.; Tonouchi, N.; Yokozeki, K.
Cloning of the xylitol dehydrogenase gene from Gluconobacter oxydans and improved production of xylitol from D-arabitol
Biosci. Biotechnol. Biochem.
67
584-591
2003
Gluconobacter oxydans
brenda
Panagiotou, G.; Kekos, D.; Macris, B.J.; Christakopoulos, P.
Purification and characterization of NAD+-dependent xylitol dehydrogenase from Fusarium oxysporum
Biotechnol. Lett.
24
2089-2092
2002
Fusarium oxysporum
-
brenda
Nidetzky, B.; Helmer, H.; Klimacek, M.; Lunzer, R.; Mayer, G.
Characterization of recombinant xylitol dehydrogenase from Galactocandida mastotermitis expressed in Escherichia coli
Chem. Biol. Interact.
143-144
533-542
2003
[Candida] sp. HA 167
brenda
Godoy de Andrade Rodrigues, D.C.; Silverio da Silva, S.; Vitolo, M.
Influence of pH on the xylose reductase activity of Candida guilliermondii during fed-batch xylitol bioproduction
J. Basic Microbiol.
42
201-206
2002
Meyerozyma guilliermondii
brenda
Tran, L.H.; Kitamoto, N.; Kawai, K.; Takamizawa, K.; Suzuki, T.
Cloning and expression of a NAD+-dependent xylitol dehydrogenase gene (xdhA) of Aspergillus oryzae
J. Biosci. Bioeng.
97
419-422
2004
Aspergillus oryzae (Q86ZV0), Aspergillus oryzae
brenda
Cortez, E.V.; Pessoa, A.Jr.; das Gracas de Almeida Felipe, M.; Roberto, I.C.; Vitolo, M.
Optimized extraction by cetyl trimethyl ammonium bromide reversed micelles of xylose reductase and xylitol dehydrogenase from Candida guilliermondii homogenate
J. Chromatogr. B
807
47-54
2004
Meyerozyma guilliermondii
brenda
Yablochkova, E.N.; Bolotnikova, O.I.; Mikhailova, N.P.; Nemova, N.N.; Ginak, A.I.
The activity of xylose reductase and xylitol dehydrogenase in yeasts
Microbiology
72
414-417
2003
Candida parapsilosis, Candida tropicalis, Candida tropicalis Y-456, Kluyveromyces marxianus, Kluyveromyces marxianus Y-488, Metahyphopichia silvanorum, Meyerozyma guilliermondii, Meyerozyma guilliermondii Y-1017, Pachysolen tannophilus, Scheffersomyces shehatae, Scheffersomyces shehatae Y-1632, Scheffersomyces stipitis, Sungouiella intermedia, [Candida] diddensiae, [Candida] diddensiae F-3
brenda
Karhumaa, K.; Hahn-Haegerdal, B.; Gorwa-Grauslund, M.F.
Investigation of limiting metabolic steps in the utilization of xylose by recombinant Saccharomyces cerevisiae using metabolic engineering
Yeast
22
359-368
2005
Saccharomyces cerevisiae
brenda
Ber, E.; Wartmann, T.; Schmidt, S.; Bode, R.; Gellissen, G.; Kunze, G.
Characterization of the AXDH gene and the encoded xylitol dehydrogenase from the dimorphic yeast Arxula adeninivorans
Antonie van Leeuwenhoek
87
233-243
2005
Blastobotrys adeninivorans (Q6KAV2), Blastobotrys adeninivorans
brenda
Ko, B.S.; Kim, J.; Kim, J.H.
Production of xylitol from D-xylose by a xylitol dehydrogenase gene-disrupted mutant of Candida tropicalis
Appl. Environ. Microbiol.
72
4207-4213
2006
Candida tropicalis
brenda
Mayerhoff, Z.D.; Roberto, I.C.; Franco, T.T.
Response surface methodology as an approach to determine the optimal activities of xylose reductase and xylitol dehydrogenase enzymes from Candida mogii
Appl. Microbiol. Biotechnol.
70
761-767
2006
Osmozyma mogii
brenda
Rodrigues, R.C.; Sene, L.; Matos, G.S.; Roberto, I.C.; Pessoa, A.; Felipe, M.G.
Enhanced xylitol production by precultivation of Candida guilliermondii cells in sugarcane bagasse hemicellulosic hydrolysate
Curr. Microbiol.
53
53-59
2006
Meyerozyma guilliermondii
brenda
Watanabe, S.; Kodaki, T.; Makino, K.
Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc
J. Biol. Chem.
280
10340-10349
2005
Scheffersomyces stipitis (P22144), Scheffersomyces stipitis
brenda
Virginio da Silva, D.D.; Felipe, M.
Effect of glucose:xylose ratio on xylose reductase and xylitol dehydrogenase activities from Candida guilliermondii in sugarcane bagasse hydrolysate
J. Chem. Technol. Biotechnol.
81
1294-1300
2006
Meyerozyma guilliermondii
-
brenda
Ehrensberger, A.H.; Elling, R.A.; Wilson, D.K.
Structure-guided engineering of xylitol dehydrogenase cosubstrate specificity
Structure
14
567-575
2006
Gluconobacter oxydans (Q8GR61), Gluconobacter oxydans
brenda
Dmytruk, O.V.; Voronovsky, A.Y.; Abbas, C.A.; Dmytruk, K.V.; Ishchuk, O.P.; Sibirny, A.A.
Overexpression of bacterial xylose isomerase and yeast host xylulokinase improves xylose alcoholic fermentation in the thermotolerant yeast Hansenula polymorpha
FEMS Yeast Res.
8
165-173
2008
Ogataea angusta
brenda
Toivari, M.H.; Ruohonen, L.; Miasnikov, A.N.; Richard, P.; Penttila, M.
Metabolic engineering of Saccharomyces cerevisiae for conversion of D-glucose to xylitol and other five-carbon sugars and sugar alcohols
Appl. Environ. Microbiol.
73
5471-5476
2007
Scheffersomyces stipitis
brenda
Karhumaa, K.; Fromanger, R.; Hahn-Haegerdal, B.; Gorwa-Grauslund, M.
High activity of xylose reductase and xylitol dehydrogenase improves xylose fermentation by recombinant Saccharomyces cerevisiae
Appl. Microbiol. Biotechnol.
73
1039-1046
2007
Saccharomyces cerevisiae
brenda
Granstroem, T.B.; Izumori, K.; Leisola, M.
A rare sugar xylitol. Part I: The biochemistry and biosynthesis of xylitol
Appl. Microbiol. Biotechnol.
74
277-281
2007
[Candida] sp. HA 167
brenda
Klimacek, M.; Hellmer, H.; Nidetzky, B.
Catalytic mechanism of Zn2+-dependent polyol dehydrogenases: kinetic comparison of sheep liver sorbitol dehydrogenase with wild-type and Glu154-Cys forms of yeast xylitol dehydrogenase
Biochem. J.
404
421-429
2007
[Candida] sp. HA 167, Ovis aries
brenda
Poonperm, W.; Takata, G.; Morimoto, K.; Granstroem, T.B.; Izumori, K.
Production of L-xylulose from xylitol by a newly isolated strain of Bacillus pallidus Y25 and characterization of its relevant enzyme xylitol dehydrogenase
Enzyme Microb. Technol.
40
1206-1212
2007
Aeribacillus pallidus, Aeribacillus pallidus Y25
-
brenda
Annaluru, N.; Watanabe, S.; Pack, S.P.; Saleh, A.A.; Kodaki, T.; Makino, K.
Thermostabilization of Pichia stipitis xylitol dehydrogenase by mutation of structural zinc-binding loop
J. Biotechnol.
129
717-722
2007
Scheffersomyces stipitis
brenda
Hou, J.; Shen, Y.; Li, X.P.; Bao, X.M.
Effect of the reversal of coenzyme specificity by expression of mutated Pichia stipitis xylitol dehydrogenase in recombinant Saccharomyces cerevisiae
Lett. Appl. Microbiol.
45
184-189
2007
Scheffersomyces stipitis
brenda
Krahulec, S.; Klimacek, M.; Nidetzky, B.
Engineering of a matched pair of xylose reductase and xylitol dehydrogenase for xylose fermentation by Saccharomyces cerevisiae
Biotechnol. J.
4
684-694
2009
[Candida] sp. HA 167
brenda
Branco, R.; dos Santos, J.; Sarrouh, B.; Rivaldi, J.; Pessoa Jr., A.; da Silva, S.
Profiles of xylose reductase, xylitol dehydrogenase and xylitol production under different oxygen transfer volumetric coefficient values
J. Chem. Technol. Biotechnol.
84
326-330
2009
Meyerozyma guilliermondii, Meyerozyma guilliermondii FTI 20037
-
brenda
Gurpilhares, D.B.; Hasmann, F.A.; Pessoa, A.; Roberto, I.C.
The behavior of key enzymes of xylose metabolism on the xylitol production by Candida guilliermondii grown in hemicellulosic hydrolysate
J. Ind. Microbiol. Biotechnol.
36
87-93
2009
Meyerozyma guilliermondii
brenda
Petschacher, B.; Nidetzky, B.
Altering the coenzyme preference of xylose reductase to favor utilization of NADH enhances ethanol yield from xylose in a metabolically engineered strain of Saccharomyces cerevisiae
Microb. Cell Fact.
7
9
2008
[Candida] sp. HA 167
brenda
Tiwari, M.K.; Moon, H.J.; Jeya, M.; Lee, J.K.
Cloning and characterization of a thermostable xylitol dehydrogenase from Rhizobium etli CFN42
Appl. Microbiol. Biotechnol.
87
571-581
2010
Rhizobium etli (Q2K0Q7)
brenda
Mahmud, A.; Hattori, K.; Hongwen, C.; Kitamoto, N.; Suzuki, T.; Nakamura, K.; Takamizawa, K.
NAD+-dependent xylitol dehydrogenase (xdhA) and L-arabitol-4-dehydrogenase (ladA) deletion mutants of Aspergillus oryzae for improved xylitol production
Biotechnol. Lett.
35
769-777
2013
Aspergillus oryzae, Aspergillus oryzae (Q86ZV0), Aspergillus oryzae KBN616, Aspergillus oryzae KBN616 (Q86ZV0)
brenda
Kim, S.R.; Kwee, N.R.; Kim, H.; Jin, Y.S.
Feasibility of xylose fermentation by engineered Saccharomyces cerevisiae overexpressing endogenous aldose reductase (GRE3), xylitol dehydrogenase (XYL2) and xylulokinase (XYL3) from Scheffersomyces stipitis
FEMS Yeast Res.
13
312-321
2013
Scheffersomyces stipitis (P22144), Scheffersomyces stipitis
brenda
Zhang, J.; Li, S.; Xu, H.; Zhou, P.; Zhang, L.; Ouyang, P.
Purification of xylitol dehydrogenase and improved production of xylitol by increasing XDH activity and NADH supply in Gluconobacter oxydans
J. Agric. Food Chem.
61
2861-2867
2013
Gluconobacter oxydans, Gluconobacter oxydans NH-10
-
brenda
Krahulec, S.; Klimacek, M.; Nidetzky, B.
Analysis and prediction of the physiological effects of altered coenzyme specificity in xylose reductase and xylitol dehydrogenase during xylose fermentation by Saccharomyces cerevisiae
J. Biotechnol.
158
192-202
2012
Saccharomyces cerevisiae
brenda
Zong, H.; Zhang, C.; Zhuge, B.; Lu, X.; Fang, H.; Sun, J.
Effects of xylitol dehydrogenase (XYL2) on xylose fermentation by engineered Candida glycerinogenes
Biotechnol. Appl. Biochem.
64
590-599
2017
Scheffersomyces stipitis
brenda
Qi, X.H.; Zhu, J.F.; Yun, J.H.; Lin, J.; Qi, Y.L.; Guo, Q.; Xu, H.
Enhanced xylitol production: Expression of xylitol dehydrogenase from Gluconobacter oxydans and mixed culture of resting cell
J. Biosci. Bioeng.
122
257-262
2016
Gluconobacter oxydans (A0A141BGH5), Gluconobacter oxydans, Gluconobacter oxydans CGMCC 1.49 (A0A141BGH5), Gluconobacter oxydans CGMCC 1.49
brenda
Weyda, I.; Luebeck, M.; Ahring, B.K.; Luebeck, P.S.
Point mutation of the xylose reductase (XR) gene reduces xylitol accumulation and increases citric acid production in Aspergillus carbonarius
J. Ind. Microbiol. Biotechnol.
41
733-739
2014
Aspergillus carbonarius, Aspergillus carbonarius ITEM 5010
brenda
Zhang, C.; Zong, H.; Zhuge, B.; Lu, X.; Fang, H.; Zhuge, J.
Integrative expression vectors for overexpression of xylitol dehydrogenase (XYL2) in osmotolerant yeast, Candida glycerinogenes WL2002-5
J. Ind. Microbiol. Biotechnol.
42
113-124
2015
Scheffersomyces stipitis (P22144), Scheffersomyces stipitis
brenda
Khattab, S.M.; Saimura, M.; Kodaki, T.
Boost in bioethanol production using recombinant Saccharomyces cerevisiae with mutated strictly NADPH-dependent xylose reductase and NADP+-dependent xylitol dehydrogenase
J. Biotechnol.
165
153-156
2013
Scheffersomyces stipitis (P22144), Scheffersomyces stipitis
brenda
Yamasaki-Yashiki, S.; Komeda, H.; Hoshino, K.; Asano, Y.
Molecular analysis of NAD+-dependent xylitol dehydrogenase from the zygomycetous fungus Rhizomucor pusillus and reversal of the coenzyme preference
Biosci. Biotechnol. Biochem.
78
1943-1953
2014
Rhizomucor pusillus (S6BFC0), Rhizomucor pusillus, Rhizomucor pusillus NBRC 4578 (S6BFC0), Rhizomucor pusillus NBRC 4578
brenda
Zhang, J.; Li, S.; Xu, H.; Zhou, P.; Zhang, L.; Ouyang, P.
Purification of xylitol dehydrogenase and improved production of xylitol by increasing XDH activity and NADH supply in Gluconobacter oxydans
J. Agric. Food Chem.
61
2861-2867
2013
Gluconobacter oxydans (Q8GR61), Gluconobacter oxydans, Gluconobacter oxydans NH-10 (Q8GR61)
brenda
Mahmud, A.; Hattori, K.; Hongwen, C.; Kitamoto, N.; Suzuki, T.; Nakamura, K.; Takamizawa, K.
Xylitol production by NAD+-dependent xylitol dehydrogenase (xdhA)- and L-arabitol-4-dehydrogenase (ladA)-disrupted mutants of Aspergillus oryzae
J. Biosci. Bioeng.
115
353-359
2013
Aspergillus oryzae (Q86ZV0), Aspergillus oryzae, Aspergillus oryzae KBN616 (Q86ZV0)
brenda
Tani, T.; Taguchi, H.; Akamatsu, T.
Analysis of metabolisms and transports of xylitol using xylose- and xylitol-assimilating Saccharomyces cerevisiae
J. Biosci. Bioeng.
123
613-620
2017
Scheffersomyces stipitis
brenda
Zhang, G.C.; Turner, T.L.; Jin, Y.S.
Enhanced xylose fermentation by engineered yeast expressing NADH oxidase through high cell density inoculums
J. Ind. Microbiol. Biotechnol.
44
387-395
2017
Scheffersomyces stipitis (P22144), Scheffersomyces stipitis ATCC 58785 (P22144)
brenda
Liu, L.; Zeng, W.; Du, G.; Chen, J.; Zhou, J.
Identification of NAD-dependent xylitol dehydrogenase from Gluconobacter oxydans WSH-003
ACS omega
4
15074-15080
2019
Gluconobacter oxydans, Gluconobacter oxydans WSH-003
brenda
Jo, J.H.; Park, Y.C.; Jin, Y.S.; Seo, J.H.
Construction of efficient xylose-fermenting Saccharomyces cerevisiae through a synthetic isozyme system of xylose reductase from Scheffersomyces stipitis
Biores. Technol.
241
88-94
2017
Scheffersomyces stipitis (P22144), Scheffersomyces stipitis ATCC 58785 (P22144), Scheffersomyces stipitis NBRC 10063 (P22144), Scheffersomyces stipitis NRRL Y-11545 (P22144)
brenda
Cunha, J.T.; Soares, P.O.; Romani, A.; Thevelein, J.M.; Domingues, L.
Xylose fermentation efficiency of industrial Saccharomyces cerevisiae yeast with separate or combined xylose reductase/xylitol dehydrogenase and xylose isomerase pathways
Biotechnol. Biofuels
12
20
2019
Saccharomyces cerevisiae (Q07993), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q07993)
brenda
Fan, E.S.; Lu, K.W.; Wen, R.C.; Shen, C.R.
Photosynthetic reduction of xylose to xylitol using cyanobacteria
Biotechnol. J.
15
e1900354
2020
Scheffersomyces stipitis (P22144), Scheffersomyces stipitis ATCC 58785 (P22144), Scheffersomyces stipitis NBRC 10063 (P22144), Scheffersomyces stipitis NRRL Y-11545 (P22144)
brenda
Mouro, A.; Santos, A.; Agnolo, D.; Gubert, G.; Bon, E.; Rosa, C.; Fonseca, C.; Stambuk, B.
Combining xylose reductase from Spathaspora arborariae with xylitol dehydrogenase from Spathaspora passalidarum to promote xylose consumption and fermentation into xylitol by Saccharomyces cerevisiae
Fermentation
6
72
2020
Spathaspora passalidarum, Spathaspora passalidarum UFMG-CM-Y474
-
brenda
Sukpipat, W.; Komeda, H.; Prasertsan, P.; Asano, Y.
Purification and characterization of xylitol dehydrogenase with L-arabitol dehydrogenase activity from the newly isolated pentose-fermenting yeast Meyerozyma caribbica 5XY2
J. Biosci. Bioeng.
123
20-27
2017
Meyerozyma caribbica (A0A1B4XTS0), Meyerozyma caribbica, Meyerozyma caribbica 5XY2 (A0A1B4XTS0), Meyerozyma caribbica 5XY2
brenda
Han, X.; Hu, X.; Zhou, C.; Wang, H.; Li, Q.; Ouyang, Y.; Kuang, X.; Xiao, D.; Xiang, Q.; Yu, X.; Li, X.; Gu, Y.; Zhao, K.; Chen, Q.; Ma, M.
Cloning and functional characterization of xylitol dehydrogenase genes from Issatchenkia orientalis and Torulaspora delbrueckii
J. Biosci. Bioeng.
130
29-35
2020
Pichia kudriavzevii (A0A3S7PMB5), Pichia kudriavzevii, Pichia kudriavzevii QLB_09 (A0A3S7PMB5), Scheffersomyces stipitis (P22144), Scheffersomyces stipitis, Scheffersomyces stipitis ATCC 58785 (P22144), Scheffersomyces stipitis NBRC 10063 (P22144), Scheffersomyces stipitis NRRL Y-11545 (P22144), Torulaspora delbrueckii (A0A3S7PMC4), Torulaspora delbrueckii, Torulaspora delbrueckii BLQ_03 (A0A3S7PMC4)
brenda
Guo, J.; Huang, S.; Chen, Y.; Guo, X.; Xiao, D.
Heterologous expression of Spathaspora passalidarum xylose reductase and xylitol dehydrogenase genes improved xylose fermentation ability of Aureobasidium pullulans
Microb. Cell Fact.
17
64
2018
Spathaspora passalidarum (G3AIB3), Spathaspora passalidarum (G3AIP8), Spathaspora passalidarum, Spathaspora passalidarum 11-Y1 (G3AIB3), Spathaspora passalidarum 11-Y1 (G3AIP8), Spathaspora passalidarum NRRL Y-27907 (G3AIP8)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.9)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
