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
-
uric
-
lignocellulosic
- pentose
- candida
- molybdenum
-
xylose-fermenting
- allopurinol
- hypoxanthine
-
xanthinuria
-
xylose-utilizing
- hydrolysate
- l-arabitol
- guilliermondii
- bagasse
-
bioethanol
- l-arabinose
-
hemicellulosic
- marxianus
- scheffersomyces
-
rosy
- d-sorbitol
-
oxygen-limited
- l-xylulose
- mocos
- tannophilus
- oxydans
- ribitol
- molecular biology
- gluconobacter
- pachysolen
- pseudoobscura
-
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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Cofactor
Cofactor on EC 1.1.1.9 - D-xylulose reductase
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NAD+
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stereochemistry of hydrogen transfer from xylitol, ribitol or sorbitol to NAD+ is of the (R)- or A-type
NAD+
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xylitol oxidation favors NAD+ over NADP+, but xylulose reduction favors NADPH over NADH
NAD+
NAD+ specificity is largely conferred by Asp38, which interacts with the hydroxyls of the adenosine ribose
NAD+
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dependent on, the wild-type enzyme prefers NAD+, while a modified mutant enzyme is also able to utilize NADP+ in the D-xylitol oxidation reaction
NAD+
the deduced XDH gene product possesses an NAD-binding glycine-rich Rossmann fold domain [GXGXXG] present in MDR superfamily
NAD+
strictly dependent on, residues Val180, Asp200, and Lys205 are responsible for NAD+ binding. Especially, Asp200 in TdXyl2p determines the specificity for NAD+, which forms double-hydrogen bonds to the hydroxyl groups in the ribosyl moiety of NAD+
NAD+
strictly dependent on, residues Val192, Asp212, and Lys217 are responsible for NAD+ binding. Especially, Asp212 in IoXyl2p determines the specificity for NAD+, which forms double-hydrogen bonds to the hydroxyl groups in the ribosyl moiety of NAD+
NADP+
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xylitol oxidation favors NAD+ over NADP+, but xylulose reduction favores NADPH over NADH
NADP+
wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity
NADP+
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the wild-type enzyme prefers NAD+, while a modified mutant enzyme is also able to utilize NADP+ in the D-xylitol oxidation reaction
additional information
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at high concentrations of xylitol 1.5% as effective as NAD+
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additional information
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at high concentrations of xylitol 1.5% as effective as NAD+
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additional information
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at high concentrations of xylitol 1.5% as effective as NAD+
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additional information
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no oxidation of ribitol or sorbitol with NADP+
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additional information
activity with NADP+ is 4% of the activity with NAD+
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additional information
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XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity
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additional information
NADP+ is a poor cofactor giving 3.1% activity compared to NAD+
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additional information
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NADP+ is a poor cofactor giving 3.1% activity compared to NAD+
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additional information
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the enzyme exhibits high preference for NAD+ as the cofactor, while no activity with NADP+, FAD, or pyrroloquinoline quinone is observed
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