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
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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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General Information
General Information on EC 1.1.1.9 - D-xylulose reductase
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evolution
malfunction
metabolism
physiological function
additional information
the enzyme belongs to a medium-chain dehydrogenase/reductase (MDR) superfamily and a subfamily of polyol dehydrogenase, PDH
evolution
the conserved coenzyme binding motif (GxGxxG) and zinc-ADH signature (GHExxGxxxxxGxxV) are observed in the amino acid sequence of RpXDH at position 181-186 and 70-84 and are completely conserved among RpXDH, XDHs, and SDHs from other filamentous fungi and yeasts
evolution
XDH has a TGXXGXXG NAD(H)-binding motif and a YXXXK active site motif, and belongs to the short-chain dehydrogenase/ reductase family
evolution
the enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily and polyol dehydrogenase (PDH) subfamily. The enzyme contains the typical NAD+-binding motif GxGxxG of MDR family enzymes
evolution
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the enzyme contains a NAD(P)-binding motif and a classical active site motif belonging to the short-chain dehydrogenase family
evolution
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the enzyme belongs to a medium-chain dehydrogenase/reductase (MDR) superfamily and a subfamily of polyol dehydrogenase, PDH
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evolution
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the enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily and polyol dehydrogenase (PDH) subfamily. The enzyme contains the typical NAD+-binding motif GxGxxG of MDR family enzymes
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evolution
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the conserved coenzyme binding motif (GxGxxG) and zinc-ADH signature (GHExxGxxxxxGxxV) are observed in the amino acid sequence of RpXDH at position 181-186 and 70-84 and are completely conserved among RpXDH, XDHs, and SDHs from other filamentous fungi and yeasts
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evolution
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the enzyme contains a NAD(P)-binding motif and a classical active site motif belonging to the short-chain dehydrogenase family
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evolution
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XDH has a TGXXGXXG NAD(H)-binding motif and a YXXXK active site motif, and belongs to the short-chain dehydrogenase/ reductase family
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deletin of gene xdhA and gene ladA and or both lead mutants with decreased dehydrogenase activities and increased xylitol production, overview
malfunction
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deletin of gene xdhA and gene ladA and or both lead mutants with decreased dehydrogenase activities and increased xylitol production, overview
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key enzymes for xylitol production in yeasts are xylose reductase and xylitol dehydrogenase, overview
metabolism
the redox balance between xylose reductase (XR) and xylitol dehydrogenase (XDH) is thought to be an important factor in effective xylose fermentation
metabolism
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in order to overcome xylitol accumulation in Aspergillus carbonarius, a K274R point mutation is introduced into the xylose reductase with the aim of changing the specificity toward NADH. Fermentation with the mutant strain (grown on D-xylose as the sole carbon source) shows a 2.8fold reduction in xylitol accumulation and 4.5fold increase in citric acid production compared to the wild-type strain. The fact that the mutant strain shows decreased xylitol levels is assumed to be associated with the capability of the mutated xylose reductase to use NADH generated by the xylitol dehydrogenase XDH, thus preventing the inhibition of XDH by the high levels of NADH and ensuring the flux of D-xylose through the pathway
metabolism
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the cofactor imbalance between the NAD(P)H-dependent wild type XR and NAD+-dependent XDH can create an intracellular redox imbalance, leading to an accumulation of NADH and a shortage of NAD+ necessary for the XDH reaction. The likely increase in intracellular xylitol concentration favors xylitol excretion, which reduces the ethanol yield by Saccharomyces cerevisiae
metabolism
xylitol dehydrogenase catalyzes the second step of D-xylose metabolism
metabolism
biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
metabolism
one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
metabolism
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xylitol dehydrogenase catalyzes the second step of D-xylose metabolism
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metabolism
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in order to overcome xylitol accumulation in Aspergillus carbonarius, a K274R point mutation is introduced into the xylose reductase with the aim of changing the specificity toward NADH. Fermentation with the mutant strain (grown on D-xylose as the sole carbon source) shows a 2.8fold reduction in xylitol accumulation and 4.5fold increase in citric acid production compared to the wild-type strain. The fact that the mutant strain shows decreased xylitol levels is assumed to be associated with the capability of the mutated xylose reductase to use NADH generated by the xylitol dehydrogenase XDH, thus preventing the inhibition of XDH by the high levels of NADH and ensuring the flux of D-xylose through the pathway
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metabolism
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one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
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metabolism
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biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
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metabolism
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one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
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metabolism
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biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
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metabolism
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one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
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metabolism
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biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
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strictly NADPH-dependent XR with mutated strict NADP+-dependent XDH are more effective in increasing bioethanol production and decreasing xylitol accumulation than the NAD+-dependent wild-type XDH, overview
physiological function
enzyme XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity directly limiting the overall conversion process of D-xylose fermentation to ethanol by Gluconobacter oxydans
physiological function
the organism catabolizes L-arabinose as well as D-glucose and D-xylose. The highest production amounts of ethanol from D-glucose, xylitol from D-xylose, and L-arabitol from L-arabinose were 0.45 g/g D-glucose, 0.60 g/g D-xylose, and 0.61 g/g L-arabinose with 21.7 g/l ethanol, 20.2 g/l xylitol, and 30.3 g/l L-arabitol, respectively. The enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
physiological function
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the organism catabolizes L-arabinose as well as D-glucose and D-xylose. The highest production amounts of ethanol from D-glucose, xylitol from D-xylose, and L-arabitol from L-arabinose were 0.45 g/g D-glucose, 0.60 g/g D-xylose, and 0.61 g/g L-arabinose with 21.7 g/l ethanol, 20.2 g/l xylitol, and 30.3 g/l L-arabitol, respectively. The enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
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physiological function
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enzyme XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity directly limiting the overall conversion process of D-xylose fermentation to ethanol by Gluconobacter oxydans
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XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity limiting the the overall conversion process, improvement by recombinant expression of enzyme and glucose dehydrogenase cofactor regeneration enzyme
additional information
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xylitol production of wild-type and mutant strains, overview
additional information
xylitol production of wild-type and mutant strains, overview
additional information
xylitol production of wild-type and mutant strains, overview
additional information
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xylitol production of wild-type and mutant strains, overview
additional information
enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding
additional information
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enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding
additional information
enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding
additional information
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enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding
additional information
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xylitol production of wild-type and mutant strains, overview
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additional information
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xylitol production of wild-type and mutant strains, overview
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additional information
Pichia kudriavzevii QLB_09
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enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding
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additional information
Torulaspora delbrueckii BLQ_03
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enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding
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additional information
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XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity limiting the the overall conversion process, improvement by recombinant expression of enzyme and glucose dehydrogenase cofactor regeneration enzyme
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