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Information on EC 2.7.1.17 - xylulokinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P42826
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2.7.1.17 xylulokinaseSpecify your search results
Word Map
- 2.7.1.17
- xylose
- xylitol
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mcleod
- pentose
- stipitis
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lignocellulosic
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x-linked
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xylose-fermenting
- acanthocytosis
- neuroacanthocytosis
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xylose-utilizing
- l-arabinose
- transaldolase
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xylose-metabolizing
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xylazine
-
co-fermentation
-
acanthocyte
-
xylulose-5-phosphate
-
bioethanol
- chorea-acanthocytosis
- biotechnology
- synthesis
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
kinase (phosphorylating), xylulo
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kinase, xylulo- (phosphorylating)
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XK
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xylokinase(phosphorylating)
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xylulokinase
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D-xylulokinase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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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
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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
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
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60% of the activity with D-xylulose
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?
ATP + D-xylulose
?
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overexpression of xylulokinase in Saccharomyces cerevisiae is detrimental to cell growth on xylulose but not on glucose
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?
ATP + D-xylulose
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xylulokinase activity is absent during glucose metabolism but is detectable during simultaneous utilization of xylulose and glucose
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?
ATP + D-xylulose
?
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expression level of xylulokinase can limit xylulose metabolism, although other factors are also likely to have a role
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?
ATP + D-xylulose
?
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the enzyme is involved in one of the initial steps of xylose utilization
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?
ATP + D-xylulose
ADP + D-xylulose 5-phosphate
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-
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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 + D-xylulose
?
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overexpression of xylulokinase in Saccharomyces cerevisiae is detrimental to cell growth on xylulose but not on glucose
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-
?
ATP + D-xylulose
?
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xylulokinase activity is absent during glucose metabolism but is detectable during simultaneous utilization of xylulose and glucose
-
-
?
ATP + D-xylulose
?
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expression level of xylulokinase can limit xylulose metabolism, although other factors are also likely to have a role
-
-
?
ATP + D-xylulose
?
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the enzyme is involved in one of the initial steps of xylose utilization
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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0.034 +/-0.002 U/mg, more than 2fold higher values than D-XR/XDH and D-XR/ARSdR, XK reaction forming ADP coupled with pyruvate kinase (PK) and lactate dehydrogenase (LDH) reactions, activity is measured by monitoring the oxidation of NADH at 340 nm in reaction mixture, one unit of enzyme activity is defined as the amount of enzyme that reduces or oxidizes 1 micromol NAD(P)+ or NAD(P)H per minute.
additional information
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20.6 +/-0.3 Unit/mg at 25°C, approx. 3 mM D-xylulose 5-phosphate could be produced over 10 min at 25°C from 5 mM xylulose with 0.004 mg purified xylulokinase. With 2.5 mM xylulose, about 80% of conversion occur.
additional information
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strain D-XR/ARSdR/XK, 0.030 +/-0.002 U/mg, more than two-fold higher values than D-XR/XDH and D-XR/ARSdR, reaction forming ADP coupled with pyruvate kinase (PK) and lactate dehydrogenase (LDH) reactions, activity is measured by monitoring the oxidation of NADH at 340 nm in reaction mixture, one unit of enzyme activity is defined as the amount of enzyme that reduces or oxidizes 1 micromol NAD(P)+ or NAD(P)H per minute.
additional information
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strain D452-2 D-XR/ARSdR, 0.013 +/-0.001 U/mg, reaction forming ADP coupled with pyruvate kinase (PK) and lactate dehydrogenase (LDH) reactions, activity is measured by monitoring the oxidation of NADH at 340 nm in reaction mixture, one unit of enzyme activity is defined as the amount of enzyme that reduces or oxidizes 1 micromol NAD(P)+ or NAD(P)H per minute.
additional information
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strain D452-2 D-XR/XDH, 0.014 +/-0.002 U/mg, reaction forming ADP coupled with pyruvate kinase (PK) and lactate dehydrogenase (LDH) reactions, activity is measured by monitoring the oxidation of NADH at 340 nm in reaction mixture, one unit of enzyme activity is defined as the amount of enzyme that reduces or oxidizes 1 micromol NAD(P)+ or NAD(P)H per minute.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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xylulokinase activity is absent during glucose metabolism but is detectable during simultaneous utilization of xylulose and glucose
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
harvested cells resuspended in 50 mM Tris/HCl pH 7.8, solution after ultrasonically disruption centrifuged at 10000 *g for 30 min at 4°C, supernatant passed through immobilized metal affinity chromatography (5 ml) using the His-tag introduced into the C-terminal region of XK, purified enzyme dialyzed against 50 mM Tris/Hcl (pH 7.8) containing 12.5% (w/v) glycerol
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain D452-2, DNA from Saccharomyces cerevisiae strain S288C, strain D-XR/ARSdR with naturally occuring XK-activity
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expressed in Saccharomyces cerevisiae strain D452-2, DNA from Saccharomyces cerevisiae strain S288C, strain D-XR/ARSdR/XK with upegulated XK-activity, entire coding sequence of XK with PGK promoter and terminator inserted into pAUR101 shuttle vector (Takara Bio, Kyoto) integrating in Saccharomyces cerevisiae strain D452-2
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expressed in Saccharomyces cerevisiae strain D452-2, DNA from Saccharomyces cerevisiae strain S288C, strain D-XR/XDH with naturally occuring enzyme-activity
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expressed in Saccharomyces cerevisiae strain D452-2, DNA from Saccharomyces cerevisiae strain S288C, strain D-XR/XDH/XK with upegulated XK-activity, entire coding sequence of XK with PGK promoter and terminator inserted into pAUR101 shuttle vector integrating in Saccharomyces cerevisiae strain D452-2
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expressed in Saccharomyces cerevisiae under the control of the glyceraldehyde 3-phosphate dehydrogenase promoter and terminator
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overexpression of the gene on Saccharomyces cerevisiae H158 and CEN-PK also expressing xylose reductase and xylitol dehydrogenase. Effect on fermentation of xylose and lignocellulosic hydrolysate
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overexpression of xylulokinase in Saccharomyces cerevisiae is detrimental to cell growth on xylulose but not on glucose
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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an effective conversion of xylulose to xylulose 5-phosphate catalyzed by the xylulokinase in Saccharomyces cerevisiae is considered to be essential for the development of an efficient and accelerated ethanol fermentation process from xylulose
synthesis
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construction of a Saccharomyces cerevisiae strain overexpressing GRE3-encoded NADPH-dependent aldose reductase and xylulokinase with a mutated strictly NADP+-dependent Pichia stipitis xylitol dehydrogenase. The recombinant strain efficiently ferments xylose and glucose mixture and the ethanol production is 21.4% higher than that of an isogenic constructed reference strain expressing Pichia stipitis xylose reductase. The yield of ethanol production increases from 0.395 g ethanol/g sugar to 0.435 g ethanol/g sugar after glucose depletion. Xylitol accumulation (0.6% of total sugar) is considerably lower than that of the reference strain (4.8% of total sugar)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johansson, B.; Christensson, C.; Hobley, T.; Hahn-Hagerdal, B.
Xylulokinase overexpression in two strains of Saccharomyces cerevisiae also expressing xylose reductase and xylitol dehydrogenase and its effect on fermentation of xylose and lignocellulosic hydrolysate
Appl. Environ. Microbiol.
67
4249-4255
2001
Saccharomyces cerevisiae, Saccharomyces cerevisiae CBS 8066
Richard, P.; Toivari, M.H.; Penttila, M.
The role of xylulokinase in Saccharomyces cerevisiae xylulose catabolism
FEMS Microbiol. Lett.
190
39-43
2000
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1B
Lee, T.H.; Kim, M.D.; Park, Y.C.; Bae, S.M.; Ryu, Y.W.; Seo, J.H.
Effects of xylulokinase activity on ethanol production from D-xylulose by recombinant Saccharomyces cerevisiae
J. Appl. Microbiol.
95
847-852
2003
Saccharomyces cerevisiae
Jeppsson, H.; Yu, S.; Hahn-Hagerdal, B.
Xylulose and glucose fermentation by Saccharomyces cerevisiae in chemostat culture
Appl. Environ. Microbiol.
62
1705-1709
1996
Saccharomyces cerevisiae
Wahlbom, C.F.; Cordero Otero, R.R.; van Zyl, W.H.; Hahn-Hagerdal, B.; Jonsson, L.J.
Molecular analysis of a Saccharomyces cerevisiae mutant with improved ability to utilize xylose shows enhanced expression of proteins involved in transport, initial xylose metabolism, and the pentose phosphate pathway
Appl. Environ. Microbiol.
69
740-746
2003
Saccharomyces cerevisiae
Jin, Y.S.; Ni, H.; Laplaza, J.M.; Jeffries, T.W.
Optimal growth and ethanol production from xylose by recombinant Saccharomyces cerevisiae require moderate D-xylulokinase activity
Appl. Environ. Microbiol.
69
495-503
2003
Saccharomyces cerevisiae, Scheffersomyces stipitis
Ni, H.; Laplaza, J.M.; Jeffries, T.W.
Transposon mutagenesis to improve the growth of recombinant Saccharomyces cerevisiae on D-xylose
Appl. Environ. Microbiol.
73
2061-2066
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae L2612
Lee, J.Y.; Cheong, D.E.; Kim, G.J.
A novel assay system for the measurement of transketolase activity using xylulokinase from Saccharomyces cerevisiae
Biotechnol. Lett.
30
899-904
2008
Saccharomyces cerevisiae
Matsushika, A.; Watanabe, S.; Kodaki, T.; Makino, K.; Sawayama, S.
Bioethanol production from xylose by recombinant Saccharomyces cerevisiae expressing xylose reductase, NADP(+)-dependent xylitol dehydrogenase, and xylulokinase
J. Biosci. Bioeng.
105
296-299
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae D452-2 D-XR/XDH/XK, Saccharomyces cerevisiae D452-2 D-XR/ARSdR/XK, Saccharomyces cerevisiae D452-2 D-XR/XDH, Saccharomyces cerevisiae D452-2 D-XR/ARSdR
Khattab, S.; Kodaki, T.
Efficient bioethanol production by overexpression of endogenous Saccharomyces cerevisiae xylulokinase and NADPH-dependent aldose reductase with mutated strictly NADP+-dependent Pichia stipitis xylitol dehydrogenase
Process Biochem.
49
1838-1842
2014
Saccharomyces cerevisiae
-
Hardt, N.; Kind, S.; Schoenenberger, B.; Eggert, T.; Obkircher, M.; Wohlgemuth, R.
Facile synthesis of D-xylulose-5-phosphate and L-xylulose-5-phosphate by xylulokinase-catalyzed phosphorylation
Biocatal. Biotransform.
38
35-45
2020
Saccharomyces cerevisiae (P42826), Saccharomyces cerevisiae ATCC 204508 (P42826)
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