1.1.1.B19: xylitol dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about xylitol dehydrogenase (NAD+), go to the full flat file.
Reaction
Synonyms
NAD+-dependent XDH, NAD+-dependent xylitol-dehydrogenase, NAD+-linked xylitol dehydrogenase, XDH, XYL2, xylitol 4-dehydrogenase, xylitol dehydrogenase
ECTree
1.1.1.B19 xylitol dehydrogenase (NAD+)Advanced search results
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General Information on EC 1.1.1.B19 - xylitol dehydrogenase (NAD+)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
metabolism
physiological function
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furfural is one of the typical inhibitors present in hemicellulose hydrolysate. Furfural is harmful to cell growth and biofuel production in microbes. Candida tropicalis obtains better furfural tolerance in xylose medium. The dehydrogenation of xylitol, which produces coenzyme NADH, promotes the recycle of NAD+ and facilitates the reduction of furfural. The rate of furfural degradation and half maximal inhibitory concentration for furfural of Candida tropicalis in xylose medium increases 1.68fold and 1.19fold, respectively
additional information
evolution
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the xylose metabolic pathway, i.e. XR, XDH and XK, is conserved among the xylitol-producing yeasts Spathaspora sp. JA1, Meyerozyma caribbica JA9 and Meyerozyma guilliermondii, but not in Spathaspora passalidarum, which possess two xylose reductases (XRs)
evolution
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the xylose metabolic pathway, i.e. XR, XDH and XK, is conserved among the xylitol-producing yeasts Spathaspora sp. JA1, Meyerozyma caribbica JA9 and Meyerozyma guilliermondii, but not in Spathaspora passalidarum, which possess two xylose reductases (XRs)
evolution
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the xylose metabolic pathway, i.e. XR, XDH and XK, is conserved among the xylitol-producing yeasts Spathaspora sp. JA1, Meyerozyma caribbica JA9 and Meyerozyma guilliermondii, but not in Spathaspora passalidarum, which possess two xylose reductases (XRs)
evolution
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the xylose metabolic pathway, i.e. XR, XDH and XK, is conserved among the xylitol-producing yeasts Spathaspora sp. JA1, Meyerozyma caribbica JA9 and Meyerozyma guilliermondii, but not in Spathaspora passalidarum, which possess two xylose reductases (XRs)
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evolution
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the xylose metabolic pathway, i.e. XR, XDH and XK, is conserved among the xylitol-producing yeasts Spathaspora sp. JA1, Meyerozyma caribbica JA9 and Meyerozyma guilliermondii, but not in Spathaspora passalidarum, which possess two xylose reductases (XRs)
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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
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the xylitol-producing yeast shows strictly NADPH-dependent xylose reductase and NAD+-dependent xylitol-dehydrogenase activities. This imbalance of cofactors favors the high xylitol yield. Spathaspora sp. JA1 is a strong xylitol producer, reaching product yield and productivity as high as 0.74 g/g and 0.20 g/l/h on xylose, and 0.58 g/g and 0.44 g/l/h on non-detoxified hydrolysate. Xylose assimilation analysis of the strain, overview
metabolism
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the xylitol-producing yeast shows strictly NADPH-dependent xylose reductase and NAD+-dependent xylitol-dehydrogenase activities. This imbalance of cofactors favors the high xylitol yield. Xylose assimilation analysis of the strain, overview
metabolism
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the xylitol-producing yeast shows strictly NADPH-dependent xylose reductase and NAD+-dependent xylitol-dehydrogenase activities. This imbalance of cofactors favors the high xylitol yield. Xylose assimilation analysis of the strain, overview
metabolism
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the xylitol-producing yeast shows strictly NADPH-dependent xylose reductase and NAD+-dependent xylitol-dehydrogenase activities. This imbalance of cofactors favors the high xylitol yield. Xylose assimilation analysis of the strain, overview
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metabolism
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the xylitol-producing yeast shows strictly NADPH-dependent xylose reductase and NAD+-dependent xylitol-dehydrogenase activities. This imbalance of cofactors favors the high xylitol yield. Xylose assimilation analysis of the strain, overview
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additional information
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enzyme structure homology modelling and molecular docking, active site structure analysis, the potential catalytic sites are Ser149, Tyr162, and Lys166 for xylitol and NAD+
additional information
Erwinia aphidicola SK47.001
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enzyme structure homology modelling and molecular docking, active site structure analysis, the potential catalytic sites are Ser149, Tyr162, and Lys166 for xylitol and NAD+
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