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Information on EC 2.7.1.17 - xylulokinase and Organism(s) Escherichia coli and UniProt Accession P09099
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EC Tree
2.7.1.17 xylulokinaseSpecify your search results
Word Map
- 2.7.1.17
- xylose
- xylitol
-
mcleod
- pentose
- stipitis
-
lignocellulosic
-
x-linked
-
xylose-fermenting
- acanthocytosis
- neuroacanthocytosis
-
xylose-utilizing
- l-arabinose
- transaldolase
-
xylose-metabolizing
-
xylazine
-
co-fermentation
-
acanthocyte
-
xylulose-5-phosphate
-
bioethanol
- chorea-acanthocytosis
- biotechnology
- synthesis
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
xk, xylulokinase, d-xylulokinase, d-xylulose kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-xylulokinase
-
-
-
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kinase (phosphorylating), xylulo
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-
-
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kinase, xylulo- (phosphorylating)
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-
-
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XK
-
-
-
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xylokinase(phosphorylating)
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-
-
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xylulokinase
xylulokinase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:D-xylulose 5-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9030-58-4
-
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
ATP + D-xylitol
ADP + D-xylitol-1-phosphate
-
analyzed with 31P NMR spectrum
-
-
?
ATP + D-xylitol
ADP + D-xylitol-5-phosphate
-
analyzed with 31P NMR spectrum
-
-
?
CTP + 1-deoxy-D-xylulose
CDP + 1-deoxy-D-xylulose 5-phosphate
-
18% of the activity with ATP
-
?
GTP + 1-deoxy-D-xylulose
GDP + 1-deoxy-D-xylulose 5-phosphate
-
38% of the activity with ATP
-
?
ITP + 1-deoxy-D-xylulose
IDP + 1-deoxy-D-xylulose 5-phosphate
-
26% of the activity with ATP
-
?
UTP + 1-deoxy-D-xylulose
UDP + 1-deoxy-D-xylulose 5-phosphate
-
8% of the activity with ATP
-
?
ATP + 1-deoxy-D-xylulose
ADP + 1-deoxy-D-xylulose 5-phosphate
-
-
-
?
ATP + 1-deoxy-D-xylulose
ADP + 1-deoxy-D-xylulose 5-phosphate
-
the reaction constitutes a potential salvage pathway for the generation of 1-deoxy-D-xylulose 5-phosphate from exogenous or endogenous 1-deoxy-D-xylulose as starting material for the biosynthesis of terpenoids, thiamine and pyridoxal
-
?
ATP + D-xylulose
ADP + D-xylulose 5-phosphate
-
-
-
-
r
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
ATP + 1-deoxy-D-xylulose
ADP + 1-deoxy-D-xylulose 5-phosphate
-
the reaction constitutes a potential salvage pathway for the generation of 1-deoxy-D-xylulose 5-phosphate from exogenous or endogenous 1-deoxy-D-xylulose as starting material for the biosynthesis of terpenoids, thiamine and pyridoxal
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-fluoro-xylulose
0.18 mM, strong inhibition of the ATPase activity of xylulokinase
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
radiometric system for measurement of enzyme activity in crude cell extracts
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.134
-
Pseudomonas putida S12 strain xylAB containing xylose isomerase and xylulokinase gene from Escherichia coli
additional information
additional information
-
0.07 units/mg, at 37°C, in Tris-HCl buffer (pH 7.5) 100 mM, MgCl2 10 mM, NADH 0.15 mM, sorbitol dehydrogenase 2 units, and xylose 500 mM
additional information
-
3.1 U/mg protein (native substrate 5 mM xylulose), with 0.14 U/mg protein activity when using 75 mM xylitol as substrate (activity in range of background level), activities measured from cell lysates by monitoring NADH depletion, using an assay in which pentulokinase activity is coupled to pyruvate kinase and lactate dehydrogenase activities, reaction mixture (final concentrations indicated): 71 mM TrisHCl pH 7.5, 7.1 mM MgCl2, 1 mM EDTA, 50 mM KCl, 7.1 mM KF, 5 mM KCN, 1.4 mM ATP, 1 mM phosphoenolpyruvic acid, 0.3 mM NADH, 0.7 U/ml pyruvate kinase, 1 U/ml lactate dehydrogenase, and 5 mM D-xylulose or 75 mM xylitol
additional information
-
3.8 U/mg protein (native substrate 5 mM xylulose), 0.76 U/mg protein (substrate 75 mM xylitol), activities measured from cell lysates by monitoring NADH depletion, using an assay in which pentulokinase activity is coupled to pyruvate kinase and lactate dehydrogenase activities, reaction mixture (final concentrations indicated): 71 mM TrisHCl pH 7.5, 7.1 mM MgCl2, 1 mM EDTA, 50 mM KCl, 7.1 mM KF, 5 mM KCN, 1.4 mM ATP, 1 mM phosphoenolpyruvic acid, 0.3 mM NADH, 0.7 U/ml pyruvate kinase, 1 U/ml lactate dehydrogenase, and 5 mM D-xylulose or 75 mM xylitol
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Pseudomonas strain S12 containing xylose isomerase gene and xylulokinase gene from Escherichia coli strain DH5 alpha
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using 1.5 M ammonium sulfate, 50 mM sodium citrate, pH 6, 1% (w/v) t-butanol and 25% (v/v) ethylene glycol, at 25°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D6A
19fold decreased ATPase activity compared to the wild type enzyme
additional information
additional information
-
Escherichia coli xylulokinase gene xylB is PCR-amplified from Escherichia coli genomic DNA, genes of interest are cloned downstream of a tac promoter and upstream of a transcription termination sequence into the medium copy vector pLOI3809, transforming plasmid into a DELTAxylB mutant E. coli strain (PC07)
additional information
-
Pichia stipitis xylulokinase gene (XYL3) is PCR-amplified from Pichia stipitis (strain UC7) genomic DNA, genes of interest are cloned downstream of a tac promoter and upstream of a transcription termination sequence into the medium copy vector pLOI3809, transforming plasmid into a DELTAxylB mutant Escherichia coli strain (PC07), determine whether an alternative xylulokinase (one not expected to act on xylitol) could functionally replace XylB in Escherichia coli, Xyl3 shares only 23% amino acid sequence identity with Escherichia coli XylB
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and functional expression of enzymes from Escherichia coli in Pseudomonas putida
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expressed in Escherichia coli strain PC07 with deleted xylB-gene and introduced plasmid with Escherichia coli xylB gene
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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putative use of lignocellulosic biomass as feedstock for the chemical industry
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wungsintaweekul, J.; Herz, S.; Hecht, S.; Eisenreich, W.; Feicht, R.; Rohdich, F.; Bacher, A.; Zenk, M.H.
Phosphorylation of 1-deoxy-D-xylulose by D-xylulokinase of Escherichia coli
Eur. J. Biochem.
268
310-316
2001
Escherichia coli, Escherichia coli DH5-alpha
Tritsch, D.; Hemmerlin, A.; Rohmer, M.; Bach, T.J.
A sensitive radiometric assay to measure D-xylulose kinase activity
J. Biochem. Biophys. Methods
58
75-83
2004
Escherichia coli
Yanase, H.; Sato, D.; Yamamoto, K.; Matsuda, S.; Yamamoto, S.; Okamoto, K.
Genetic engineering of Zymobacter palmae for production of ethanol from xylose
Appl. Environ. Microbiol.
73
2592-2599
2007
Escherichia coli
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
Escherichia coli, Escherichia coli DH5-alpha, Ogataea angusta
Di Luccio, E.; Petschacher, B.; Voegtli, J.; Chou, H.T.; Stahlberg, H.; Nidetzky, B.; Wilson, D.K.
Structural and kinetic studies of induced fit in xylulose kinase from Escherichia coli
J. Mol. Biol.
365
783-798
2007
Escherichia coli (P09099), Escherichia coli
Akinterinwa, O.; Cirino, P.C.
Heterologous expression of d-xylulokinase from Pichia stipitis enables high levels of xylitol production by engineered Escherichia coli growing on xylose
Metab. Eng.
11
45-55
2009
Escherichia coli
Akinterinwa, O.; Cirino, P.C.
Heterologous expression of d-xylulokinase from Pichia stipitis enables high levels of xylitol production by engineered Escherichia coli growing on xylose
Metab. Eng.
11
48-55
2009
Escherichia coli
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