2.7.1.17: xylulokinase
This is an abbreviated version!
For detailed information about xylulokinase, go to the full flat file.
Word Map on EC 2.7.1.17
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2.7.1.17
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xylose
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xylitol
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mcleod
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pentose
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stipitis
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lignocellulosic
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x-linked
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xylose-fermenting
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acanthocytosis
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neuroacanthocytosis
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xylose-utilizing
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l-arabinose
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transaldolase
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xylose-metabolizing
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xylazine
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co-fermentation
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acanthocyte
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xylulose-5-phosphate
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bioethanol
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chorea-acanthocytosis
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biotechnology
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synthesis
- 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
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co-fermentation
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acanthocyte
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xylulose-5-phosphate
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bioethanol
- chorea-acanthocytosis
- biotechnology
- synthesis
Reaction
Synonyms
1-deoxy-D-xylulokinase, ATP/polyphosphate xylulokinase, D-xululokinase, D-xylulokinase, D-xylulose kinase, DXK, Huta_2446, kinase (phosphorylating), xylulo, kinase, xylulo- (phosphorylating), TM0116, XK, XK-1, XKS1, XyiH, XYL3, XylB, xylokinase(phosphorylating), xylulokinase
ECTree
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Specific Activity
Specific Activity on EC 2.7.1.17 - xylulokinase
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0.134
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Pseudomonas putida S12 strain xylAB containing xylose isomerase and xylulokinase gene from Escherichia coli
23.5
using D-xylulose as substrate, 50 mM Tris-HCl (pH 7.5), at 25°C
46
using D-fructose as substrate, 50 mM Tris-HCl (pH 7.5), at 25°C
additional information
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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
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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
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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
additional information
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0.144 +/-0.008 U/mg protein, the transformant grown in YNB medium with 4% D-xylose showes 2-fold higher XK activity as compared to that of the wild-type strain, activity in cell extracts is determined spectrophotometrically at 37°C, assay mixture: Tris-HCl (pH 7.8) 50 mM, MgCl2 5 mM, NADH 0.2 mM, phosphoenolpyruvate 1 mM, D-xylulose 8.5 mM, lactate dehydrogenase 10 U, pyruvate kinase 0.05 U, ATP 2 mM
additional information
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0.366 +/-0.019 U/mg protein, up to 2.4-fold increase in specific activity of XK as compared to wild type strain CBS4732, XK activity in cell extracts is determined spectrophotometrically at 37°C, XK assay mixture containes Tris-HCl buffer (pH 7.8) 50 mM, MgCl2 5 mM, NADH 0.2 mM, phosphoenolpyruvate 1 mM, D-xylulose 8.5 mM, lactate dehydrogenase (EC 1.1.1.27) 10 U, pyruvate kinase (EC 2.7.1.40) 0.05 U, and ATP 2 mM, reaction is started with addition of cell extract, blank without pyruvate kinase and lactate dehydrogenase is used to minimize interference of XDH activity in Hansenula polymorpha.
additional information
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strain XRn/XDH/XK, 0.375 +/-0.021 U/mg protein, up to 2.4-fold increase in specific activity of XK as compared to wild type strain CBS4732, activity in cell extracts is determined spectrophotometrically at 37°C, assay mixture containes Tris-HCl buffer (pH 7.8) 50 mM, MgCl2 5 mM, NADH 0.2 mM, phosphoenolpyruvate 1 mM, D-xylulose 8.5 mM, lactate dehydrogenase (EC 1.1.1.27) 10 U, pyruvate kinase (EC 2.7.1.40) 0.05 U, and ATP 2 mM. The reaction is started with addition of cell extract, blank without pyruvate kinase and lactate dehydrogenase is used to minimize interference of XDH activity in Hansenula polymorpha.
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.