EC Number   |
Protein Variants |
Reference |
|---|
   1.1.1.10 | L242W/T244C |
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature |
654438 |
| 1.1.1.10 | more |
deletion of gene lxr3 leads to a significant reduction in NADPH specific LXR activity after replacement to both media containing L-arabinose |
-, 721689 |
| 1.1.1.10 | more |
engineering of strain YZJ088 for ethanol production via the NADP(H)-preferring xylose reductase-xylitol dehydrogenase pathway in the thermotolerant yeast Kluyveromyces marxianus, method overview |
-, 740346 |
| 1.1.1.10 | more |
enzyme XDH is changed from NAD+-dependent to NADP+-dependent, xylitol accumulation is reduced and ethanol production improved using protein engineering for reversing the dependency of XDH from NAD+ to NADP+. Construction of a set of recombinant Saccharomyces cerevisiae carrying a mutated strictly NADPH-dependent XR and NADP+-dependent XDH genes with overexpression of endogenous xylulokinase (XK), effects of complete NADPH/NADP+ recycling on ethanol fermentation and xylitol accumulation, overview. The mutated strains demonstrate 0% and 10% improvement in ethanol production, and reduced xylitol accumulation, ranging 34.4-54.7% compared with the control strain |
740782 |
| 1.1.1.10 | more |
Escherichia coli strain WZ04 is first constructed by a simultaneous deletion-insertion strategy involving CRISPR/Cas9 markerless gene-editing technology, replacing ptsG, xylAB and ptsF in wild-type Escherichia coli strain W3110 with three mutated xylose reductase genes (xr) from Neurospora crassa. In a second approach, the pfkA, pfkB, pgi and/or sthA genes are deleted and replaced by xr to investigate the influence of carbon flux toward the pentose phosphate pathway and/or transhydrogenase activity on NADPH generation. The deletion of pfkA/pfkB significantly improves NADPH supply, but minimally influences cell growth. The effects of insertion position and copy number of xr are examined by a quantitative real-time PCR and a shake-flask fermentation experiment. In a fed-batch fermentation experiment with a 15-l bioreactor, strain WZ51 produces 131.6 g/l xylitol from hemicellulosic hydrolysate (xylitol productivity: 2.09 g/l/h). The biotransformation process involves resting cell catalysis with pure xylose as the substrate, but not hemicellulosic hydrolysate. Cofactor ratios are measured for single gene replacement strains and strains with combinatorial gene replacements, all based on strain WZ04, overview |
-, 761647 |
| 1.1.1.10 | more |
library screening and isolation of a dhs-21 deletion mutant |
722271 |
| 1.1.1.10 | more |
several mutants per site-directed mutagenesis to change the coenzyme binding specificity, mutants showed reduced NAD+ specificity |
285666 |
| 1.1.1.10 | more |
xylitol is produced from xylose via the NADPH dependent reductase, a two-stage dynamic control over feedback regulatory mechanisms improves NADPH flux and xylitol biosynthesis in engineered Escherichia coli, method evaluation, overview. Comparison of two approaches to optimize xylitol biosynthesis: a stoichiometric approach wherein competitive fluxes are decreased, and a regulatory approach wherein the levels of key regulatory metabolites are reduced. The stoichiometric and regulatory approaches lead to a 20fold and 90fold improvement in xylitol production, respectively. Strains with reduced levels of enoyl-ACP reductase and glucose-6-phosphate dehydrogenase, lead to altered metabolite pools resulting in the activation of the membrane bound transhydrogenase and an NADPH generation pathway, consisting of pyruvate ferredoxin oxidoreductase coupled with NADPH dependent ferredoxin reductase, causing increased NADPH fluxes, despite a reduction in NADPH pools. These strains produce titers of 200 g/l of xylitol from xylose at 86% of theoretical yield in instrumented bioreactors |
761812 |
| 1.1.1.10 | N107D |
site-directed mutagenesis, active site residue mutant, inactive |
657322 |
| 1.1.1.10 | N107L |
site-directed mutagenesis, active site residue mutant, inactive |
657322 |
