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E231K
less than 0.24% wild type kcat
D151N/E222Q
loss of catalytic ability, loss of binding of Mn2+. Crystallization data
W203A
complete loss of activity
W203F
turnover is largely limited by product release for the wild-type enzyme, chemistry is significantly more rate-limiting for mutants W203F and W203Y. Mutant is more sensitive to fosmidomycin than wild-type. Mutation strongly tips the entropy-enthalpy balance of total binding energy
W203G
complete loss of activity
W203Y
turnover is largely limited by product release for the wild-type enzyme, chemistry is significantly more rate-limiting for mutants W203F and W203Y. Mutant is more sensitive to fosmidomycin than wild-type. Mutation strongly tips the entropy-enthalpy balance of total binding energy
D151N/E222Q
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loss of catalytic ability, loss of binding of Mn2+. Crystallization data
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W203A
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complete loss of activity
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W203F
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turnover is largely limited by product release for the wild-type enzyme, chemistry is significantly more rate-limiting for mutants W203F and W203Y. Mutant is more sensitive to fosmidomycin than wild-type. Mutation strongly tips the entropy-enthalpy balance of total binding energy
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W203G
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complete loss of activity
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W203Y
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turnover is largely limited by product release for the wild-type enzyme, chemistry is significantly more rate-limiting for mutants W203F and W203Y. Mutant is more sensitive to fosmidomycin than wild-type. Mutation strongly tips the entropy-enthalpy balance of total binding energy
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H219Q
site-directed mutagenesis, the mutation decreased the affinity toward the substrate 1-deoxy-D-xylulose 5-phosphate with an 8-fold increase in the Km compared to the wild-type enzyme
D152A
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, 4.1% activity compared to the wild-type enzyme
D152N
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, inactive mutant
E154D
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.28% activity compared to the wild-type enzyme
E154Q
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.008% activity compared to the wild-type enzyme
E223H
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.007% activity compared to the wild-type enzyme
E223Q
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, inactive mutant
H155A
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, 32% activity compared to the wild-type enzyme
M206A
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, 9% activity compared to the wild-type enzyme
M206V
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, inactive mutant
S153A
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.11% activity compared to the wild-type enzyme
S153N
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.76% activity compared to the wild-type enzyme
S153T
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site-directed mutagenesis, active site mutant, in sense and antisense orientation, 4.8% activity compared to the wild-type enzyme
W204A
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site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
W204F
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site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme, the mutant is active with the substrate analogue 1,2-dideoxy-D-threo-3-hexulose 6-phosphate in contrast to the wild-type enzyme
W204L
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site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
W204V
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site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
additional information
2-C-methyl-D-erythritol 4-phosphate pathway gene-disrupted Escherichia coli mutants. DXR is functionally active in Escherichia coli mutant DYM1
additional information
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2-C-methyl-D-erythritol 4-phosphate pathway gene-disrupted Escherichia coli mutants. DXR is functionally active in Escherichia coli mutant DYM1
additional information
DXR gene silencing by RNAi using Agrobacterium tumefaciens strain LBA4404, mutants phenotype, detailed analysis, overview. AaDXR-RNAi plants show no significant variation of stomatal length and density at the abaxial side of leaves. No significant alteration of floral initiation and flower opening is observed in the transgenic plants. The trichome density and area in leaves and flower buds are analyzed by fluorescence microscopy. It is evident that leaves of transgenic Artemisia annua in vegetative stage carry considerably lower density of trichomes than that of control. The trichome area of transgenic Artemisia annua is larger than that of control. During the flower formation, there is no difference of trichome density and area on flower bud surface between transgenic plants and control. Significant decline in chlorphylls Chla and Chlb is found in various growth stages of transgenic plants. Net photosynthesis rate of in DXRRNAi plants is decreased by 20.0-31.4% compared with that of the controls
additional information
functional complementation of Escherichia coli mutant lacking 1-deoxy-D-xylulose 5-phosphate reductoisomerase activity
additional information
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functional complementation of Escherichia coli mutant lacking 1-deoxy-D-xylulose 5-phosphate reductoisomerase activity
additional information
2-C-methyl-D-erythritol 4-phosphate pathway gene-disrupted Escherichia coli mutants. DXR is functionally active in Escherichia coli mutant DYM1
additional information
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2-C-methyl-D-erythritol 4-phosphate pathway gene-disrupted Escherichia coli mutants. DXR is functionally active in Escherichia coli mutant DYM1
additional information
rescuing of Escherichia coli enzyme-knockout mutants by the Ginkgo gene clone from embryonic roots
additional information
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rescuing of Escherichia coli enzyme-knockout mutants by the Ginkgo gene clone from embryonic roots
additional information
2-C-methyl-D-erythritol 4-phosphate pathway gene-disrupted Escherichia coli mutants. DXR is functionally active in Escherichia coli mutant DYM1
additional information
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2-C-methyl-D-erythritol 4-phosphate pathway gene-disrupted Escherichia coli mutants. DXR is functionally active in Escherichia coli mutant DYM1
additional information
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removal of C-terminal 18 amino acid residues has no effect on enzyme activity, affinity for substrates or sensitivity to isotopic probes
additional information
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construction of an N-terminal His6-tagged enzyme variant comprising the first 389 of 413 residues, the mutant is more stable and kinetically similar to the wild-type enzyme
additional information
expression profiles of carotenoid biosynthetic genes in leaves and seeds among three independent transgenic plants for each OsDXS2 and OsDXR construct relative to non-transgenic (NT) and stPAC plants. The endogenous expression of OsDXS1 and OsDXS2 increases up to 6.7fold and 4.0fold, respectively, following the overexpression of OsDXR, but the enhanced activity of OsDXS2 does not cause a significant increase in OsDXR expression, even though the expression of the OsPSY2 gene is significantly increased up to 5.7fold following the overexpression of OsDXS2
additional information
recombinant overexpression of PtDXR in transgenic poplars improves tolerance to abiotic and biotic stresses. Overexpression of PtDXR increases plant tolerance to salt stress, the phenotype, RWC, SOD and POD activities. Increased transcript levels of PtDXR increase in response to Septotinia populiperda, the spread and extent of pathogens in the wild-type plants are faster and greater than in the transgenic lines, based on analysis of the length and width of the largest pathogenic region, phenotype overview
additional information
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recombinant overexpression of PtDXR in transgenic poplars improves tolerance to abiotic and biotic stresses. Overexpression of PtDXR increases plant tolerance to salt stress, the phenotype, RWC, SOD and POD activities. Increased transcript levels of PtDXR increase in response to Septotinia populiperda, the spread and extent of pathogens in the wild-type plants are faster and greater than in the transgenic lines, based on analysis of the length and width of the largest pathogenic region, phenotype overview
additional information
gene complements Escherichia coli mutant deficient of 1-deoxy-D-xylulose 5-phosphate reductoisomerase
additional information
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gene complements Escherichia coli mutant deficient of 1-deoxy-D-xylulose 5-phosphate reductoisomerase
additional information
MH018577
chlorophylls and carotenoids increased in 35S::SaDXR overexpression Arabidopsis thaliana lines
additional information
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chlorophylls and carotenoids increased in 35S::SaDXR overexpression Arabidopsis thaliana lines
additional information
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transplastomic tobacco plants that overproduce enzyme show an increase in the content of various isoprenoids such as chlorophyll, alpha,beta carotene, lutein, antheraxanthin, solanesol and beta-sitosterol with qualitative change in isoprenoid composition. Growth phenotype of transplastomic strains is similar to wild-type