1.1.1.9: D-xylulose reductase
This is an abbreviated version!
For detailed information about D-xylulose reductase, go to the full flat file.
Word Map on EC 1.1.1.9
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1.1.1.9
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xanthine
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xylose
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stipitis
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pichia
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xylulokinase
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uric
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lignocellulosic
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pentose
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candida
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molybdenum
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xylose-fermenting
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allopurinol
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hypoxanthine
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xanthinuria
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xylose-utilizing
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hydrolysate
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l-arabitol
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guilliermondii
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bagasse
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bioethanol
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l-arabinose
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hemicellulosic
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marxianus
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scheffersomyces
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rosy
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d-sorbitol
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oxygen-limited
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l-xylulose
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mocos
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tannophilus
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oxydans
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ribitol
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molecular biology
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gluconobacter
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pachysolen
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pseudoobscura
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sulfurase
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shehatae
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synthesis
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biotechnology
- 1.1.1.9
- xanthine
- xylose
- stipitis
- pichia
- xylulokinase
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uric
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lignocellulosic
- pentose
- candida
- molybdenum
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xylose-fermenting
- allopurinol
- hypoxanthine
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xanthinuria
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xylose-utilizing
- hydrolysate
- l-arabitol
- guilliermondii
- bagasse
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bioethanol
- l-arabinose
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hemicellulosic
- marxianus
- scheffersomyces
-
rosy
- d-sorbitol
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oxygen-limited
- l-xylulose
- mocos
- tannophilus
- oxydans
- ribitol
- molecular biology
- gluconobacter
- pachysolen
- pseudoobscura
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sulfurase
- shehatae
- synthesis
- biotechnology
Reaction
Synonyms
2,3-cis-polyol(DPN) dehydrogenase (C3-5), D-xylulose reductase A, erythritol dehydrogenase, GmXDH, IoXyl2p, McXDH, More, NAD+-dependent XDH, NAD+-dependent xylitol dehydrogenase, NAD+-linked xylitol dehydrogenase, NAD-dependent xylitol dehydrogenase, NADH-dependent XDH, NADH-dependent xylitol dehydrogenase, nicotinamide adenine dinucleotide-dependent xylitol dehydrogenase 2, pentitol-DPN dehydrogenase, Ps-XDH, PsXDH, reductase, D-xylulose, RpXDH, slSDH, SpXYL2.2, SsXyl2p, TdXyl2p, XDH, XDH-Y25, xdhA, XL2, XYL2, XYL2.1, XYL2.2, xylitol dehydrogenase, xylitol dehydrogenase 2, xylitol-2-dehydrogenase
ECTree
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Application
Application on EC 1.1.1.9 - D-xylulose reductase
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biotechnology
molecular biology
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a high thermostability of PsXDH is obtained by subsequent site-directed mutagenesis of the structural zinc-binding loop. The best mutant in this study (C4/F98R/E101F) shows a 10.8 °C higher thermal transition temperature and 20.8 °C higher half denaturation temperature (T1/2) compared with wild-type
synthesis
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pretreatment of sugarcane bagasse hydrolysate to eliminate toxic compounds unsuitable for use as growth medium in xylitol production. Optimization of adsorption time, type of acid used, concentration and charcoal leads to a high ratio of xylose reductase, EC1.1.1.21, to xylitol dehydrogenase, EC1.1.1.9, of 4.5
biotechnology
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strain overexpressing enzyme has improved xylitol productivity, production of up to 57g/l xylitol from 225 g/l D-arabitol, via D-xylulose
biotechnology
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cells previously grown in sugar cane bagasse hemicellulosic hydrolysate are effective in enhancing xylitol production by keeping the xylose reductase (EC 1.1.1.21) activity at high levels, reducing the xylitol dehydrogenase (EC 1.1.1.9) activity and increasing xylitol volumetric productivity (26.5%) with respect to the inoculum cultivated in semidefined medium.Therefore, inoculum adaptation to sugar cane bagasse hemicellulosic hydrolysate is an important strategy to improve xylitol productivity
biotechnology
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the productivity and yield of xylitol fermentation by the XYL2-disrupted mutant are remarkably enhanced by screening suitable cosubstrates and optimizing the process
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optimization of xylitol production, using fed-batch process and controlled pH 6.0 gives maximum enzyme activity
synthesis
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use of enzyme in production of xylitol from bagasse hydrolysate, enzyme activity is higher in medium containing acetic acid than in control medium
synthesis
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use of enzyme in xylose fermentation, metabolic flux partitioning from xylitol to xylulose depends on aeration and enzyme activity, increased aeration results in less xylitol accumulation and more xylulose accumulation, increase in enzyme activity can reduce xylitol formation
synthesis
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the enzyme is useful for xylitol bioproduction, profiles, overview
synthesis
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Gluconobacter oxydans strain NH-10 is useful for production of xylitol from D-arabitol via D-xylulose
synthesis
enzyme IoXyl2p from Issatchenkia orientalis is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate
synthesis
enzyme TdXyl2p from Torulaspora delbrueckii is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate
synthesis
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the enzyme is useful for xylitol bioproduction, profiles, overview
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synthesis
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the enzyme is useful for xylitol bioproduction, profiles, overview
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synthesis
Pichia kudriavzevii QLB_09
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enzyme IoXyl2p from Issatchenkia orientalis is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate
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synthesis
Torulaspora delbrueckii BLQ_03
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enzyme TdXyl2p from Torulaspora delbrueckii is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate
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synthesis
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Gluconobacter oxydans strain NH-10 is useful for production of xylitol from D-arabitol via D-xylulose
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