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Information on EC 1.1.1.B19 - xylitol dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.B19preliminary BRENDA-supplied EC number
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EC Tree
1.1.1.B19 xylitol dehydrogenase (NAD+)Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
NAD+-dependent XDH, NAD+-dependent xylitol-dehydrogenase, NAD+-linked xylitol dehydrogenase, XDH, XYL2, xylitol 4-dehydrogenase, xylitol dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NAD+-dependent xylitol-dehydrogenase
NAD+-linked xylitol dehydrogenase
XDH
xylitol 4-dehydrogenase
xylitol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
xylitol + NAD+ = L-xylulose + NADH + H+
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SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD+ 2-oxidoreductase (L-xylulose-forming)
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-arabitol + NADH + H+
D-ribulose + NAD+
15% conversion in resting cell reaction
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?
D-iditol + NAD+
D-sorbose + NADH + H+
72% conversion in resting cell reaction
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?
D-talitol + NADH + H+
D-tagatose + NAD+
15% conversion in resting cell reaction
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?
D-threitol + NAD+
erythrulose + NADH + H+
48% conversion in resting cell reaction
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?
ribitol + NADH + H+
D-ribulose + NAD+
15% conversion in resting cell reaction
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?
xylitol + NAD+
L-xylulose + NADH + H+
50% conversion in resting cell reaction
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r
additional information
?
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no substrate: DL-rhamnitol, galactitol, allitol, DL-fucitol, L-iditol, L-threitol, DL-sorbitol, DL-mannitol, erythritol
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?
additional information
?
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Candida tropicalis can use xylose in hemicellulose hydrolysate
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additional information
?
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xylitol dehydrogenase almost exclusively uses NAD+ as cofactor in the dehydrogenation of xylitol into xylulose
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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Candida tropicalis can use xylose in hemicellulose hydrolysate
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
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xylitol dehydrogenase almost exclusively uses NAD+ as cofactor in the dehydrogenation of xylitol into xylulose
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
no significant stimulation by Na+, Cu2+, K+, Zn2+, Co2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from decaying wood samples collected in Brasilia, Distrito Federal, Brazil (S15-35'36.1'' WO47-44'28.2'')
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brenda
isolated from decaying wood samples collected in Brasilia, Distrito Federal, Brazil (S15-35'36.1'' WO47-44'28.2'')
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brenda
isolated from decaying wood samples collected in Brasilia, Distrito Federal, Brazil (S15-35'36.1'' WO47-44'28.2'')
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
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furfural is one of the typical inhibitors present in hemicellulose hydrolysate. Furfural is harmful to cell growth and biofuel production in microbes. Candida tropicalis obtains better furfural tolerance in xylose medium. The dehydrogenation of xylitol, which produces coenzyme NADH, promotes the recycle of NAD+ and facilitates the reduction of furfural. The rate of furfural degradation and half maximal inhibitory concentration for furfural of Candida tropicalis in xylose medium increases 1.68fold and 1.19fold, respectively
additional information
evolution
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the xylose metabolic pathway, i.e. XR, XDH and XK, is conserved among the xylitol-producing yeasts Spathaspora sp. JA1, Meyerozyma caribbica JA9 and Meyerozyma guilliermondii, but not in Spathaspora passalidarum, which possess two xylose reductases (XRs)
evolution
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the xylose metabolic pathway, i.e. XR, XDH and XK, is conserved among the xylitol-producing yeasts Spathaspora sp. JA1, Meyerozyma caribbica JA9 and Meyerozyma guilliermondii, but not in Spathaspora passalidarum, which possess two xylose reductases (XRs)
evolution
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the xylose metabolic pathway, i.e. XR, XDH and XK, is conserved among the xylitol-producing yeasts Spathaspora sp. JA1, Meyerozyma caribbica JA9 and Meyerozyma guilliermondii, but not in Spathaspora passalidarum, which possess two xylose reductases (XRs)
evolution
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the xylose metabolic pathway, i.e. XR, XDH and XK, is conserved among the xylitol-producing yeasts Spathaspora sp. JA1, Meyerozyma caribbica JA9 and Meyerozyma guilliermondii, but not in Spathaspora passalidarum, which possess two xylose reductases (XRs)
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evolution
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the xylose metabolic pathway, i.e. XR, XDH and XK, is conserved among the xylitol-producing yeasts Spathaspora sp. JA1, Meyerozyma caribbica JA9 and Meyerozyma guilliermondii, but not in Spathaspora passalidarum, which possess two xylose reductases (XRs)
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metabolism
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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
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the xylitol-producing yeast shows strictly NADPH-dependent xylose reductase and NAD+-dependent xylitol-dehydrogenase activities. This imbalance of cofactors favors the high xylitol yield. Spathaspora sp. JA1 is a strong xylitol producer, reaching product yield and productivity as high as 0.74 g/g and 0.20 g/l/h on xylose, and 0.58 g/g and 0.44 g/l/h on non-detoxified hydrolysate. Xylose assimilation analysis of the strain, overview
metabolism
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the xylitol-producing yeast shows strictly NADPH-dependent xylose reductase and NAD+-dependent xylitol-dehydrogenase activities. This imbalance of cofactors favors the high xylitol yield. Xylose assimilation analysis of the strain, overview
metabolism
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the xylitol-producing yeast shows strictly NADPH-dependent xylose reductase and NAD+-dependent xylitol-dehydrogenase activities. This imbalance of cofactors favors the high xylitol yield. Xylose assimilation analysis of the strain, overview
metabolism
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the xylitol-producing yeast shows strictly NADPH-dependent xylose reductase and NAD+-dependent xylitol-dehydrogenase activities. This imbalance of cofactors favors the high xylitol yield. Xylose assimilation analysis of the strain, overview
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metabolism
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the xylitol-producing yeast shows strictly NADPH-dependent xylose reductase and NAD+-dependent xylitol-dehydrogenase activities. This imbalance of cofactors favors the high xylitol yield. Xylose assimilation analysis of the strain, overview
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additional information
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enzyme structure homology modelling and molecular docking, active site structure analysis, the potential catalytic sites are Ser149, Tyr162, and Lys166 for xylitol and NAD+
additional information
Erwinia aphidicola SK47.001
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enzyme structure homology modelling and molecular docking, active site structure analysis, the potential catalytic sites are Ser149, Tyr162, and Lys166 for xylitol and NAD+
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). XYL2_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
363
0
38521
Swiss-Prot
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene XDH, DNA and amino acid sequence determination and analysis, sequence comparisons
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gene XDH, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
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 mutation 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
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recombinant expression in Bacillus subtilis, coexpression with the water-forming enzyme NADH oxidase (NOX) for NAD+ recycling leading to 3.4fold increased XDH activity
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gene XDH, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
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gene XDH, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
production of L-xylulose from xylitol using a resting cell reaction leads to 35% L-xylulose within 24 h, starting from 5% xylitol as initial concentration
synthesis
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enzyme XDH from Erwinia aphidicola can be useful for production of L-xylulose, a rare ketose, for apllication in pharmaceutical and food industries
synthesis
Erwinia aphidicola SK47.001
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enzyme XDH from Erwinia aphidicola can be useful for production of L-xylulose, a rare ketose, for apllication in pharmaceutical and food industries
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takata, G.; Poonperm, W.; Morimoto, K.; Izumori, K.
Cloning and overexpression of the xylitol dehydrogenase gene from Bacillus pallidus and its application to L-xylulose production
Biosci. Biotechnol. Biochem.
74
1807-1813
2010
Aeribacillus pallidus (E0D583)
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)
brenda
Promdonkoy, P.; Siripong, W.; Downes, J.J.; Tanapongpipat, S.; Runguphan, W.
Systematic improvement of isobutanol production from D-xylose in engineered Saccharomyces cerevisiae
AMB Express
9
160
2019
Candida tropicalis, Candida tropicalis PWY1353, Scheffersomyces stipitis
brenda
Wang, S.; He, Z.; Yuan, Q.
Xylose enhances furfural tolerance in Candida tropicalis by improving NADH recycle
Chem. Eng. Sci.
158
37-40
2017
Candida tropicalis
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brenda
Trichez, D.; Steindorff, A.S.; Soares, C.E.V.F.; Formighieri, E.F.; Almeida, J.R.M.
Physiological and comparative genomic analysis of new isolated yeasts Spathaspora sp. JA1 and Meyerozyma caribbica JA9 reveal insights into xylitol production
FEMS Yeast Res.
19
foz034
2019
Meyerozyma caribbica, Meyerozyma caribbica JA9, Meyerozyma guilliermondii, Meyerozyma guilliermondii NRRL Y-324, no activity in Spathaspora passalidarum strain NRRL Y-27 907, Spathaspora sp. JA1
brenda
Li, M.; Zhu, W.; Meng, Q.; Miao, M.; Zhang, T.
Characterization of xylitol 4-dehydrogenase from Erwinia aphidicola and its co-expression with NADH oxidase in Bacillus subtilis
Process Biochem.
104
92-100
2021
Erwinia aphidicola, Erwinia aphidicola SK47.001
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brenda
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