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Enzyme Nomenclature
Information on EC 1.1.1.175 - D-xylose 1-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.175
Word Map on EC 1.1.1.175
- 1.1.1.175
- d-xylonate
- nadp+
-
caulobacter
- crescentus
-
nadp+-dependent
- d-glucose
- reesei
- pentose
- xylitol
-
glucose-fructose
-
dehydratase
- l-arabinose
-
trichoderma
- xylulose
- alpha-ketoglutarate
-
titre
-
azospirillum
- d-ribose
- marismortui
-
haloferax
-
gluconobacter
- brasiliense
- oxydans
-
halophilic
- lactonase
-
haloarcula
-
dihydrodiol
-
non-food
-
kluyveromyces
- volcanii
- d-galactose
- synthesis
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
1.1.1.175
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RECOMMENDED NAME
GeneOntology No.
D-xylose 1-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-xylose + NAD+ = D-xylonolactone + NADH + H+
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene xylB, the enzyme is encoded in the xylose-inducible xylXABCD operon
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gene xylB, the enzyme is encoded in the xylose-inducible xylXABCD operon
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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-xylose + NAD+
?
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+)
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-
?
D-xylose + NAD+
?
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+)
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-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
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the enzyme is involved in the pathway for D-xylose metabolism, overview
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-
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
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the enzyme strongly prefers D-xylose as a substrate, overview
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-
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
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the enzyme is involved in the pathway for D-xylose metabolism, overview
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-
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
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the enzyme strongly prefers D-xylose as a substrate, overview
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-
r
D-xylose + NAD+
D-xylonolactone + NADH + H+
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highly specific for both substrates
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?
D-xylose + NAD+
D-xylonolactone + NADH + H+
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highly specific for both substrates
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?
D-xylose + NAD+
D-xylonolactone + NADH + H+
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highly specific for both substrates
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?
D-xylose + NAD+
D-xylonolactone + NADH + H+
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highly specific for both substrates
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?
D-xylose + NAD+
D-xylonolactone + NADH + H+
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specific hydrogen transfer for pro-R -A site
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?
additional information
?
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L-arabinose is a poor substrate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
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the enzyme is involved in the pathway for D-xylose metabolism, overview
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-
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
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the enzyme is involved in the pathway for D-xylose metabolism, overview
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-
r
D-xylose + NAD+
D-xylonolactone + NADH + H+
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highly specific for both substrates
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?
D-xylose + NAD+
D-xylonolactone + NADH + H+
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highly specific for both substrates
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?
D-xylose + NAD+
D-xylonolactone + NADH + H+
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highly specific for both substrates
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?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
highly specific for both substrates
-
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
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specific hydrogen transfer for pro-R -A site
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
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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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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inducible enzyme synthesis by growth in D-xylose-containing medium
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inducible enzyme synthesis by growth in D-xylose-containing medium
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inducible enzyme synthesis by growth in D-xylose-containing medium
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inducible enzyme synthesis by growth in D-xylose-containing medium
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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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
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gene xylB, recombinnat expression in Saccharomyces cerevisiae strain VVT B-67002
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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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
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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
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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; 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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.175)
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