Information on EC 1.1.1.179 - D-xylose 1-dehydrogenase (NADP+)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.179
-
RECOMMENDED NAME
GeneOntology No.
D-xylose 1-dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-xylose + NADP+ = D-xylono-1,5-lactone + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
xylose degradation III
-
-
d-xylose degradation
-
-
Pentose and glucuronate interconversions
-
-
SYSTEMATIC NAME
IUBMB Comments
D-xylose:NADP+ 1-oxidoreductase
Also acts, more slowly, on L-arabinose and D-ribose.
CAS REGISTRY NUMBER
COMMENTARY hide
83534-37-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
DS70 strain H26
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
camphorquinone + NADPH
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
show the reaction diagram
-
-
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
show the reaction diagram
D-glucose + NAD(P)+
D-gluconolactone + NAD(P)H
show the reaction diagram
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
D-glucose + NADP+
D-gluconolactone + NADPH + H+
show the reaction diagram
reaction is catalyzed with 70fold lower catalytic efficiency (kcat/KM) compared to activity with D-xylose + NADP*
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
show the reaction diagram
D-ribose + NADP+
?
show the reaction diagram
D-ribose + NADP+
? + NADPH
show the reaction diagram
A8BT09
low activity
-
-
?
D-ribose + NADP+
D-ribonolactone + NADPH + H+
show the reaction diagram
reaction is catalyzed with 1.8fold lower catalytic efficiency (kcat/KM) compared to activity with D-xylose + NADP*
-
-
?
D-xylose + NAD(P)+
D-xylonolactone + NAD(P)H
show the reaction diagram
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
show the reaction diagram
-
very low activity compared to NADP+
-
-
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
show the reaction diagram
Vmax/Km for NADP+ is 7fold higher than Vmax/KM for NAD+
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
show the reaction diagram
D-xylose + NADP+
D-xylonolactone + NADPH + H+
show the reaction diagram
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH
show the reaction diagram
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
show the reaction diagram
-
44% of the activity with D-xylose
-
-
?
trans-benzene dihydrodiol + NADP+
?
show the reaction diagram
trans-naphthalene dihydrodiol + NADP+
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
show the reaction diagram
D-xylose + NADP+
D-xylonolactone + NADPH + H+
show the reaction diagram
Q5UY95
initial step in xylose degradation
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
show the reaction diagram
-
44% of the activity with D-xylose
-
-
?
additional information
?
-
Q9TQS6
D-xylose dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
maximal activity at 1.5 M
Mg2+
A8BT09
-
MgCl2
maximal activity at 100 M
NaCl
maximal activity at 1.5 M
Zn2+
-
2 mol Zn2+ per monomer
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxyacetophenone
-
High salt concentration
-
recombinant H79Q mutant
-
isoascorbic acid
competitive inhibitor
L-Lyxose
-
-
NAD+
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
-
increase in activity about 2fold
MgCl2
-
increase in activity about 4fold
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
54
2-deoxy-D-glucose
-
-
0.1 - 0.51
Camphorquinone
130
D-arabinose
-
-
140
D-galactose
-
-
5.7 - 198
D-glucose
2.3 - 27
D-ribose
1.2 - 90
D-xylose
57
L-arabinose
-
-
0.36 - 5.03
NAD+
0.0006 - 24
NADP+
0.028
NADPH
-
camphorquinone, mutant H79Q
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22
2-deoxy-D-glucose
Sus scrofa
-
-
9
D-arabinose
Sus scrofa
-
-
12
D-galactose
Sus scrofa
-
-
5.7 - 273
D-glucose
40 - 360
D-ribose
0.4 - 356
D-xylose
45
L-arabinose
Sus scrofa
-
-
1.5
NAD+
Paenarthrobacter nicotinovorans
-
28C, pH 7.8
10.5
NADP+
Paenarthrobacter nicotinovorans
-
28C, pH 7.8
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043
D-glucose
Haloarcula marismortui
Q5UY95
pH 8.3, 37C
35
1.57
D-ribose
Haloarcula marismortui
Q5UY95
pH 8.3, 37C
292
0.98 - 2.97
D-xylose
115
0.298
NAD+
Paenarthrobacter nicotinovorans
-
28C, pH 7.8
7
32
NADP+
Paenarthrobacter nicotinovorans
-
28C, pH 7.8
10
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3 - 5.5
-
wild-type and mutant H79Q
7.1
-
-
7.6
-
-
7.8
with D-glucose as substrate
18
-
substrate camphorquinone, mutant H79Q
24.1
with D-xylose as substrate
33
-
substrate camphorquinone
additional information
A8BT09
substrate specificity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.1
A8BT09
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
more than 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
activity increases exponentially with temperature between 25C and 45C. 50C: optimum
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
-
gel filtration
70000
-
about, gel filtration
165000
native enzyme
175000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
A8BT09
x * 42720, sequence calculation
homotetramer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are obtained at 19.9C in a culture plate via the vapour-diffusion method, crystal structure of dimeric D-xylose dehydrogenase complexed with the inhibitor isoascorbic acid is determined at 2.59 A resolution
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
on Ni-NTA column and by gel filtration
recombinant enzyme and mutants Y180F, H79Q
-
recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
A8BT09
the recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA subcloned in expression vector pRset, overexpression in Escherichia coli
-
cloned into pET19b, resulting plasmid harvested from Escherichia coli JM109, sequenced, and transformed into Escherichia coli Rosetta(DE3)-pLysS expression strain; expression in Escherichia coli
expressed in Escherichia coli
-
expression in Kluyveromyces lactis
-
gene xyd1, DNA and amino acid sequence determination and analysis, functional expression of the His-tagged enzyme in Saccharomyces cerevisiae
A8BT09
overexpression in Escherichia coli
wild-type protein and mutants are expressed in Escherichia coli BL21 (DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A36D
site-directed mutagenesis
D280A
by site-directed mutagenesis
F154A
by site-directed mutagenesis
F279A
by site-directed mutagenesis
H76Q
by site-directed mutagenesis
H79Q
by site-directed mutagenesis
K97M
by site-directed mutagenesis
K97R
by site-directed mutagenesis
R37A
site-directed mutagenesis
R37D
site-directed mutagenesis
R41A
by site-directed mutagenesis
R41D
by site-directed mutagenesis
W125Y
by site-directed mutagenesis
W254A
by site-directed mutagenesis
W254Y
by site-directed mutagenesis
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
production of up to19 g D-xylonate per litre in Kluyveromyces lactis expressing gene xyd1 upon growth on D-galactosel and D-xylose. D-Xylose uptake is not affected by deletion of either the D-xylose reductase XYL1 or a putative xylitol dehydrogenase encoding gene XYL2 in xyd1 expressing strains
Show AA Sequence (102 entries)
Please use the Sequence Search for a certain query.