1.1.1.430: D-xylose reductase (NADH)
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For detailed information about D-xylose reductase (NADH), go to the full flat file.
Reaction
Synonyms
CbXR, CT-XR, dsXR, NAD(P)H-dependent D-xylose reductase, NADH-dependent XR, NADPH-preferring xylose reductase, PsXR, XYL1, XYL1.1, XYL1.2, xylose reductase
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1.1.1.430 D-xylose reductase (NADH)Advanced search results
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Engineering on EC 1.1.1.430 - D-xylose reductase (NADH)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K274R
K21A
-
mutation reverses the cofactor specificity from major NADP- to NAD-dependent
K270N
-
mutation reverses the cofactor specificity from major NADP- to NAD-dependent
K270S/N272P/S271G/R276F
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the mutant shows a 25fold preference toward NADH over NADPH by a factor of about 13fold, or an improvement of about 42fold, as measured by the ratio of the specificity constant kcat/Km coenzyme. Compared with the wild-type, the kcat(NADH) is slightly lower, while the kcat(NADPH) decreases by a factor of about 10
H113A
mutation causes a 10000-100000fold decrease in the rate constant for hydride transfer from NADH to 9,10-phenanthrenequinone, whose value in the wild-type enzyme is about 800 per s
K274R/N276D
L80A
mutation causes a 10000-100000fold decrease in the rate constant for hydride transfer from NADH to 9,10-phenanthrenequinone, whose value in the wild-type enzyme is about 800 per s
Y51A
mutation causes a 10000-100000fold decrease in the rate constant for hydride transfer from NADH to 9,10-phenanthrenequinone, whose value in the wild-type enzyme is about 800 per s
additional information
K274R
-
mutation introduced to change the specificity toward NADH. Fermentation with the mutant strain shows a 2.8fold reduction in xylitol accumulation and 4.5fold increase in citric acid production compared to the wild-type strain
K274R
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mutation introduced to change the specificity toward NADH. Fermentation with the mutant strain shows a 2.8fold reduction in xylitol accumulation and 4.5fold increase in citric acid production compared to the wild-type strain
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K274R/N276D
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structure-guided site-directed mutagenesis, change of the coenzyme preference of the xyluose reductase about 170fold from NADPH in the wild-type to NADH, which, in spite of the structural modifications introduced, has retained the original catalytic efficiency for reduction of xylose by NADH
K274R/N276D
NADH-specific mutant, Saccharomyces cerevisiae expressing mutant K274R/N276D exhibits intracellular activities of 0.94 U/mg 1.07 U/mg with NADPH and NADH, respectively
additional information
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the native xylose reductase gene Kmxyl1 of the Kluyveromyces marxianus strain YHJ010 is substituted with xylose reductase or its mutants N272D, K21A/N272D, or K270M from Pichia stipitis, i.e. Scheffersomyces stipitis, resulting in Kluyveromyces marxianus strains YZB013, YZB014, and YZB015. The ability of the resultant recombinant strains to assimilate xylose to produce xylitol and ethanol at elevated temperature is greatly improved, overview. But the strain YZB015 expressing a mutant PsXR K21A/N272D, with which co-enzyme preference is completely reversed from NADPH to NADH, fails to ferment due to the low expression
additional information
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the native xylose reductase gene Kmxyl1 of the Kluyveromyces marxianus strain YHJ010 is substituted with xylose reductase or its mutants N272D, K21A/N272D, or K270M from Pichia stipitis, i.e. Scheffersomyces stipitis, resulting in Kluyveromyces marxianus strains YZB013, YZB014, and YZB015. The ability of the resultant recombinant strains to assimilate xylose to produce xylitol and ethanol at elevated temperature is greatly improved, overview. But the strain YZB015 expressing a mutant PsXR K21A/N272D, with which co-enzyme preference is completely reversed from NADPH to NADH, fails to ferment due to the low expression
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additional information
the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
additional information
the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
additional information
-
the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
additional information
a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
