1.1.1.10: L-xylulose reductase
This is an abbreviated version!
For detailed information about L-xylulose reductase, go to the full flat file.
Word Map on EC 1.1.1.10
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1.1.1.10
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stipitis
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candida
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pichia
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biomass
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pentose
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xylulokinase
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lignocellulosic
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d-xylose
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xylose-fermenting
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hydrolysate
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nadph-dependent
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tenuis
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xylose-utilizing
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scheffersomyces
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l-arabinose
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hemicellulosic
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aldo-keto
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bioethanol
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guilliermondii
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aldose
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tropicalis
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shehatae
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oxygen-limited
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kluyveromyces
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transaldolase
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furfural
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tannophilus
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pachysolen
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bagasse
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nadph-preferring
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reesei
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marxianus
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co-fermentation
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1.1.1.21
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xylose-assimilating
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debaryomyces
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arabitol
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pharmacology
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synthesis
- 1.1.1.10
- stipitis
- candida
- pichia
- biomass
- pentose
- xylulokinase
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lignocellulosic
- d-xylose
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xylose-fermenting
- hydrolysate
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nadph-dependent
- tenuis
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xylose-utilizing
- scheffersomyces
- l-arabinose
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hemicellulosic
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aldo-keto
-
bioethanol
- guilliermondii
- aldose
- tropicalis
- shehatae
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oxygen-limited
- kluyveromyces
- transaldolase
- furfural
- tannophilus
- pachysolen
- bagasse
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nadph-preferring
- reesei
- marxianus
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co-fermentation
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1.1.1.21
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xylose-assimilating
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debaryomyces
- arabitol
- pharmacology
- synthesis
Reaction
Synonyms
DCXR, dicarbonyl/L-xylulose reductase, L-xylulose reductase, LXR, LXR3, More, NAD(P)H-dependent xylose reductase, NADP(+)-dependent xylitol dehydrogenase, NADP(H)-preferring xylitol dehydrogenase, NADP+-dependent xylitol dehydrogenase, NADP+-linked xylitol dehydrogenase, P31h, P34H, reductase, L-xylulose, RpLXR, Rplxr3, XDH, XR, XylB, xylitol dehydrogenase, xylose reductase
ECTree
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Engineering
Engineering on EC 1.1.1.10 - L-xylulose reductase
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D238E
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site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
D238E/L242W
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site-directed mutagenesis, mutation leads to complete prevention of cold inactivation, mutant exists in tetrameric form at low temperature
D238E/L242W/T244C
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site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
L242W
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site-directed mutagenesis, mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
L242W/T244C
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site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
T244C
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site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
H146L
K153M
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site-directed mutagenesis, active site mutant, complete loss of activity
L143F
N190V/W191S
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site-directed mutagenesis, almost complete loss of L-xylulose reductase activity
N190V/W191S/Q137M/L143F/H146L
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site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows high 3-ketosteroid reductase activity
Q137M
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site-directed mutagenesis, altered activity, stable against cold inactivation
Q137M/F241L
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site-directed mutagenesis, altered activity, sensitive to cold inactivation like the wild-type enzyme
Q137M/L143F
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site-directed mutagenesis, increased Km for L-xylulose compared to the wild-type
Q137M/L143F/H146L
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site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows 3-ketosteroid reductase activity
S136A
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site-directed mutagenesis, active site mutant, complete loss of activity
W191F
W191S
Y149F
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site-directed mutagenesis, active site mutant, complete loss of activity
D207/I208R/F209S
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kcat/Km of mutant enzyme for NAD+ dropps 15fold compared with the native enzyme, kcat/Km for NADP+ increases up to 4100fold
S96C/S99C/Y102C/D207A/I208R/F209S
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mutation produces a further 4fold improvement in the kcat/Km for NADP+ compared to mutant enzyme D207/I208R/F209S
additional information
H146L
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IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 7.8fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 6.7fold higher than wild-type value
L143F
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IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 8.3fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 1.9fold higher than wild-type value
W191F
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IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 3.4fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 7.3fold higher than wild-type value
W191S
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IC50-value for 4-methyl-[1,2,3]-thiadiazole-5-carboxylic acid benzyloxyamide is 13fold higher than wild-type value, IC50-value for 4-methylthiophene-2-carboxylic acid N'-(2,3,3-trichloroacryloyl)-hydrazide is 1.5fold lower than wild-type value
library screening and isolation of a dhs-21 deletion mutant
additional information
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library screening and isolation of a dhs-21 deletion mutant
additional information
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
additional information
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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
additional information
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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
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additional information
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
additional information
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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
additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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several mutants per site-directed mutagenesis to change the coenzyme binding specificity, mutants showed reduced NAD+ specificity
additional information
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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
additional information
deletion of gene lxr3 leads to a significant reduction in NADPH specific LXR activity after replacement to both media containing L-arabinose
additional information
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deletion of gene lxr3 leads to a significant reduction in NADPH specific LXR activity after replacement to both media containing L-arabinose
additional information
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deletion of gene lxr3 leads to a significant reduction in NADPH specific LXR activity after replacement to both media containing L-arabinose
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