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Information on EC 1.1.1.175 - D-xylose 1-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.175
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.175 D-xylose 1-dehydrogenase
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
- 1.1.1.175
- d-xylonate
- nadp+
- dehydrogenases
- l-arabinose
-
caulobacter
- crescentus
- reesei
-
nadp+-dependent
- pentose
- d-glucose
-
trichoderma
-
glucose-fructose
-
xylonic
- alpha-ketoglutarate
-
azospirillum
- xylulose
-
non-food
-
co-immobilization
- oxydans
- hexoses
-
haloarcula
- marismortui
-
haloferax
- volcanii
- brasiliense
-
gluconobacter
- lactonase
-
dihydrodiol
- synthesis
showSynonyms
d-xylose dehydrogenase, d-xylose 1-dehydrogenase, d-xdh, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(NAD)-linked D-xylose dehydrogenase
-
-
-
-
D-xylose 1-dehydrogenase
D-xylose dehydrogenase
NAD+-dependent xylose dehydrogenase
NAD-D-xylose dehydrogenase
-
-
-
-
XDH
XylB
additional information
D-xylose dehydrogenase
-
-
-
-
additional information
-
the enzyme belongs to the short-chain dehydrogenase/reductase family
additional information
-
the enzyme belongs to the short-chain dehydrogenase/reductase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-xylose + NAD+ = D-xylonolactone + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
D-xylose degradation V
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SYSTEMATIC NAME
IUBMB Comments
D-xylose:NAD+ 1-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
62931-20-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-xylono-1,4-lactone + NADH + H+
D-xylose + NAD+
-
Substrates: -
Products: -
Products: -
r
D-xylose + NAD+
D-xylono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
?
Substrates: 79% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+)
Products: -
Products: -
?
D-xylose + NAD+
?
Substrates: 79% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+)
Products: -
Products: -
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: the enzyme is involved in the pathway for D-xylose metabolism, overview
Products: -
Products: -
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: the enzyme strongly prefers D-xylose as a substrate, overview
Products: -
Products: -
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: the enzyme is involved in the pathway for D-xylose metabolism, overview
Products: -
Products: -
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
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Substrates: the enzyme strongly prefers D-xylose as a substrate, overview
Products: -
Products: -
r
D-xylose + NAD+
D-xylonolactone + NADH + H+
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Substrates: highly specific for both substrates
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: specific hydrogen transfer for pro-R -A site
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-arabinose is a poor substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-arabinose is a poor substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-xylono-1,4-lactone + NADH + H+
D-xylose + NAD+
-
Substrates: -
Products: -
Products: -
r
D-xylose + NAD+
D-xylono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: the enzyme is involved in the pathway for D-xylose metabolism, overview
Products: -
Products: -
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: the enzyme is involved in the pathway for D-xylose metabolism, overview
Products: -
Products: -
r
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: highly specific for both substrates
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: specific hydrogen transfer for pro-R -A site
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene xylB, the enzyme is encoded in the xylose-inducible xylXABCD operon
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brenda
gene xylB, the enzyme is encoded in the xylose-inducible xylXABCD operon
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
inducible enzyme synthesis by growth in D-xylose-containing medium
brenda
-
inducible enzyme synthesis by growth in D-xylose-containing medium
-
brenda
-
inducible enzyme synthesis by growth in D-xylose-containing medium
brenda
-
inducible enzyme synthesis by growth in D-xylose-containing medium
-
brenda
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (916 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.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
engineering of non-conventional yeast Pichia kudriavzevii strain VTT C-79090T to recombinantly express the D-xylose dehydrogenase coding gene from Caulobacter crescentus. With this single modification the recombinant strain VTT C-79090T produces up to 171 g/l of D-xylonate from 171 g/l D-xylose at a rate of 1.4 g/l/h and a high yield, which is comparable with D-xylonate production by Gluconobacter oxydans or Pseudomonas sp. The productivity of the strain is also remarkably high at low pH, producing 146 g/l D-xylonate at pH 3.0. Comparison to production of D-xylonate from Saccharomyces cerevisiae strain VTT B-67002 expressing the gene from Caulobacter crescentus, overview
additional information
-
engineering of non-conventional yeast Pichia kudriavzevii strain VTT C-79090T to recombinantly express the D-xylose dehydrogenase coding gene from Caulobacter crescentus. With this single modification the recombinant strain VTT C-79090T produces up to 171 g/l of D-xylonate from 171 g/l D-xylose at a rate of 1.4 g/l/h and a high yield, which is comparable with D-xylonate production by Gluconobacter oxydans or Pseudomonas sp. The productivity of the strain is also remarkably high at low pH, producing 146 g/l D-xylonate at pH 3.0. Comparison to production of D-xylonate from Saccharomyces cerevisiae strain VTT B-67002 expressing the gene from Caulobacter crescentus, overview
additional information
both D-xylono-gamma-lactone and D-xylonate are produced when the Caulobacter crescentus gene xylB encoding D-xylose dehydrogenase is expressed in Saccharomyces cerevisiae, with or without co-expressionof xylC (D-xylonolactonase). XylC facilitates rapid opening of the lactone and more D-xylonate is initially produced than in its absence. In vivo [1H]NMR analysis of cell extracts, culture media and intact cells is used for analysis. The lactone and linear forms of D-xylonic acid are produced, accumulated intracellularly, and partially exported within 1560 min after D-xylose provision. Co-expression of xylB and xylC leads to rapid loss of pHluorin fluorescence and loss of vitality during production of D-xylonate. Loss of vitality in the presence of D-xylose is correlated to the extracellular pH, but fluorescence is lost from xylB and xylC expressing cells regardless of the extracellular condition. Method optimization, overview
additional information
-
engineering of non-conventional yeast Pichia kudriavzevii strain VTT C-79090T to recombinantly express the D-xylose dehydrogenase coding gene from Caulobacter crescentus. With this single modification the recombinant strain VTT C-79090T produces up to 171 g/l of D-xylonate from 171 g/l D-xylose at a rate of 1.4 g/l/h and a high yield, which is comparable with D-xylonate production by Gluconobacter oxydans or Pseudomonas sp. The productivity of the strain is also remarkably high at low pH, producing 146 g/l D-xylonate at pH 3.0. Comparison to production of D-xylonate from Saccharomyces cerevisiae strain VTT B-67002 expressing the gene from Caulobacter crescentus, overview
-
additional information
-
both D-xylono-gamma-lactone and D-xylonate are produced when the Caulobacter crescentus gene xylB encoding D-xylose dehydrogenase is expressed in Saccharomyces cerevisiae, with or without co-expressionof xylC (D-xylonolactonase). XylC facilitates rapid opening of the lactone and more D-xylonate is initially produced than in its absence. In vivo [1H]NMR analysis of cell extracts, culture media and intact cells is used for analysis. The lactone and linear forms of D-xylonic acid are produced, accumulated intracellularly, and partially exported within 1560 min after D-xylose provision. Co-expression of xylB and xylC leads to rapid loss of pHluorin fluorescence and loss of vitality during production of D-xylonate. Loss of vitality in the presence of D-xylose is correlated to the extracellular pH, but fluorescence is lost from xylB and xylC expressing cells regardless of the extracellular condition. Method optimization, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene xylB, recombinnat expression in Pichia kudriavzevii strain VTT C-79090T
gene xylB, recombinnat expression in Saccharomyces cerevisiae strain VVT B-67002
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
expression of gene xylB in Saccharomyces cerevisiae results in production of 17 g D-xylonate/l at 0.23g/l/h from 23 g D-xylose/l. D-Xylonate accumulates intracellularly to 70 mg/g, xylitol to 18 mg/g. Cells expressing D-xylonolactone lactonase xylC from Caulobacter crescentus with xylB initially produce more extracellular D-xylonate than cells lacking xylC at both pH5.5 and pH3, and sustain higher production at pH3. Cell vitality and viability decreases during D-xylonate production at pH 3.0
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamanaka, K.; Gino, M.
Purification and properties of D-xylose dehydrogenase in bacteria
Hakko Kogaku Kaishi
57
322-331
1979
Pseudomonas sp.
-
brenda
Yamanaka, K.; Gino, M.; Kaneda, R.
A specific NAD-D-xylose dehydrogenase from Arthrobacter sp.
Agric. Biol. Chem.
41
1493-1499
1977
Arthrobacter sp., Arthrobacter sp. 588
-
brenda
Dahms, A.S.; Russo, J.
D-Xylose dehydrogenase
Methods Enzymol.
89
226-228
1982
Pseudomonas sp., Pseudomonas sp. MSU-1
brenda
Mostad, S.B.; Helming, H.L.; Groom, C.; Glasfeld, A.
The stereospecificity of hydrogen transfer to NAD(P)+ catalyzed by lactol dehydrogenases
Biochem. Biophys. Res. Commun.
233
681-686
1997
Sus scrofa
brenda
Bonete, M.J.; Pire, C.; Llorca, F.I.; Camacho, M.L.
Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterization and N-terminal sequence
FEBS Lett.
383
227-229
1996
Haloferax mediterranei (Q977U7), Haloferax mediterranei DSM 1411 (Q977U7)
brenda
Stephens, C.; Christen, B.; Fuchs, T.; Sundaram, V.; Watanabe, K.; Jenal, U.
Genetic analysis of a novel pathway for D-xylose metabolism in Caulobacter crescentus
J. Bacteriol.
189
2181-2185
2007
Caulobacter vibrioides, Caulobacter vibrioides NA1000
brenda
Toivari, M.; Nygard, Y.; Kumpula, E.P.; Vehkomaeki, M.L.; Bencina, M.; Valkonen, M.; Maaheimo, H.; Andberg, M.; Koivula, A.; Ruohonen, L.; Penttilae, M.; Wiebe, M.G.
Metabolic engineering of Saccharomyces cerevisiae for bioconversion of D-xylose to D-xylonate
Metab. Eng.
14
427-436
2012
Caulobacter vibrioides (B8H1Z0), Caulobacter vibrioides
brenda
Nygard, Y.; Maaheimo, H.; Mojzita, D.; Toivari, M.; Wiebe, M.; Resnekov, O.; Gustavo Pesce, C.; Ruohonen, L.; Penttilae, M.
Single cell and in vivo analyses elucidate the effect of xylC lactonase during production of D-xylonate in Saccharomyces cerevisiae
Metab. Eng.
25
238-247
2014
Caulobacter vibrioides (B8H1Z0), Caulobacter vibrioides NA1000 (B8H1Z0)
brenda
Toivari, M.; Vehkomaeki, M.; Nygard, Y.; Penttilae, M.; Ruohonen, L.; Wiebe, M.
Low pH D-xylonate production with Pichia kudriavzevii
Biores. Technol.
133
555-562
2013
Caulobacter vibrioides (B8H1Z0), Caulobacter vibrioides, Caulobacter vibrioides NA1000 (B8H1Z0)
brenda
Sanchez-Moreno, I.; Benito-Arenas, R.; Montero-Calle, P.; Hermida, C.; Garcia-Junceda, E.; Fernandez-Mayoralas, A.
Simple and practical multigram synthesis of D-xylonate using a recombinant xylose dehydrogenase
ACS Omega
4
10593-10598
2019
Caulobacter vibrioides
brenda
Lee, C.; Jordan, D.; Stoller, J.; Kibblewhite, R.; Wagschal, K.
Biochemical characterization of Caulobacter crescentus xylose dehydrogenase
Int. J. Biol. Macromol.
118
1362-1367
2018
Caulobacter vibrioides
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.175)
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