2.2.1.7: 1-deoxy-D-xylulose-5-phosphate synthase
This is an abbreviated version!
For detailed information about 1-deoxy-D-xylulose-5-phosphate synthase, go to the full flat file.
Word Map on EC 2.2.1.7
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2.2.1.7
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isoprenoids
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carotenoid
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reductoisomerase
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methylerythritol
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isopentenyl
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terpenoids
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phytoene
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plastidial
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2-c-methyl-d-erythritol
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dimethylallyl
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2-c-methyl-d-erythritol-4-phosphate
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non-mevalonate
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fosmidomycin
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thdp-dependent
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isoprene
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apocarotenoids
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ggpps
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diphosphate-dependent
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clomazone
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4-diphosphate
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mevalonate-independent
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analysis
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drug development
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medicine
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synthesis
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agriculture
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biotechnology
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industry
- 2.2.1.7
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isoprenoids
-
carotenoid
- reductoisomerase
- methylerythritol
-
isopentenyl
-
terpenoids
- phytoene
- plastidial
-
2-c-methyl-d-erythritol
-
dimethylallyl
- 2-c-methyl-d-erythritol-4-phosphate
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non-mevalonate
- fosmidomycin
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thdp-dependent
- isoprene
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apocarotenoids
- ggpps
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diphosphate-dependent
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clomazone
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4-diphosphate
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mevalonate-independent
- analysis
- drug development
- medicine
- synthesis
- agriculture
- biotechnology
- industry
Reaction
Synonyms
1-D-deoxy-D-threo-2-pentulose 5-phosphate synthetase, 1-D-deoxyxylulose 5-phosphate synthase, 1-deoxy-D-threo-pentulose synthase, 1-deoxy-D-xylulose 5-phosphate synthase, 1-deoxy-D-xylulose 5-phosphate synthase 1, 1-deoxy-D-xylulose 5-phosphate synthase 2, 1-deoxy-D-xylulose 5-phosphate synthetase, 1-deoxy-D-xylulose-5-phosphate pyruvate lyase, 1-deoxy-D-xylulose-5-phosphate synthase, 1-deoxy-D-xylulose-5-phosphate synthase 1, 1-deoxy-D-xylulose-5-phosphate synthetase, 1-desoxy-D-xylulose-5-phosphate synthase, CSDXS, D-1-deoxyxylulose 5-phosphate synthase, deoxyxylulose 5-phosphate synthase, deoxyxylulose-5-phosphate synthase, deoxyxylulose-5-phosphate synthetase, DXP, DXP synthase, DXP-synthase, DXPase, DXPS, DXS, DXS-I, DXS-II, DXS1, dxs11, DXS2, DXS3, EC 4.1.3.37, GbDXS1, GbDXS2, glyceraldehydes 3-phosphate-pyruvate ligase, GmDXS1, MtDXS1, MtDXS2, OsDXS1, OsDXS2, OsDXS3, PaDXS1, PaDXS2A, PaDXS2B, PdDXS1, PdDXS2, synthase, 1-deoxy-D-xylulose 5-phosphate
ECTree
2.2.1.7 1-deoxy-D-xylulose-5-phosphate synthaseAdvanced search results
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results (Engineering
Engineering on EC 2.2.1.7 - 1-deoxy-D-xylulose-5-phosphate synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H48A
mutant protein with lost activity, below 0.1% of specific activity compared with that of the wild-type
D430A
H304A
the mutant produces a catalytically defective enzyme. The mutant shows 12.1% and 11.4% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively
H340A
the mutant shows 7 and 2% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
H434A
H82A
N181A
the mutant shows 9 and 70% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
R420A
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thiamine diphosphate is significantly stabilized on the variant compared to the wild type enzyme in the absence of acceptor substrate. The substitution reduces affinity for D-glyceraldehyde 3-phosphate
R423K
the mutant shows 7 and 250% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
R478A
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thiamine diphosphate is significantly stabilized on the variant compared to the wild type enzyme in the absence of acceptor substrate. The substitution reduces affinity for D-glyceraldehyde 3-phosphate
Y392F
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thiamine diphosphate is significantly stabilized on the variant compared to the wild type enzyme in the absence of acceptor substrate. The substitution reduces affinity for D-glyceraldehyde 3-phosphate
Y395A
the mutant shows 4 and 80% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
Y395F
the mutant shows 9 and 60% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
D430A
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while the kcat for D430A mutant remains relatively unchanged, the KM for pyruvate and D-glyceraldehyde 3-phosphate increases 1.9 and 2.4times, respectively. The mutant shows 97.3% and 97.5% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively
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H304A
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the mutant produces a catalytically defective enzyme. The mutant shows 12.1% and 11.4% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively
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H434A
H82A
N181A
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the mutant shows 9 and 70% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
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R423K
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the mutant shows 7 and 250% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
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H49Q
mutant enzyme shows no detectable DXP-synthase activity, this demonstrates the key role of H49 for enzyme activity
R420A
the mutation has no apparent effect on the affinities of nitroso substrates in C-N bond formation
R478A
K284N
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single nucleotide polymorphism, significantly associated with Muscat-flavoured varieties. Substitution influences the enzyme kinetics by increasing the catalytic efficiency and also dramatically affects monoterpene levels upon heterologous expression
additional information
D430A
the mutant shows 9 and 50% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
D430A
while the kcat for D430A mutant remains relatively unchanged, the KM for pyruvate and D-glyceraldehyde 3-phosphate increases 1.9 and 2.4times, respectively. The mutant shows 97.3% and 97.5% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively
H434A
the electrostatic effects that accompany the H434A mutation have a clear destabilizing effect on substrate binding while enhancing turnover. The mutant shows 133.8% and 121.5% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively
H434A
the mutant shows 30 and more than 20% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
H82A
the KM values for the mutant for both D-glyceraldehyde 3-phosphate and pyruvate are similar to the wild type enzyme. The mutant shows 9 and 7% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
H82A
the mutant produces a catalytically defective enzyme. The mutant shows 5.1% and 4.7% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively
H434A
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the mutant shows 30 and more than 20% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
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H434A
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the electrostatic effects that accompany the H434A mutation have a clear destabilizing effect on substrate binding while enhancing turnover. The mutant shows 133.8% and 121.5% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively
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H82A
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the KM values for the mutant for both D-glyceraldehyde 3-phosphate and pyruvate are similar to the wild type enzyme. The mutant shows 9 and 7% of wild type activity for D-glyceraldehyde 3-phosphate and pyruvate, respectively
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H82A
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the mutant produces a catalytically defective enzyme. The mutant shows 5.1% and 4.7% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively
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R478A
the mutation has no apparent effect on the affinities of nitroso substrates in C-N bond formation
R478A
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the mutant shows reduced affinity for D-glyceraldehyde 3-phosphate compared to the wild type enzyme
additional information
recombinant Escherichia coli harboring the dxs gene produce more CoQ8 compared with the wildtype Escherichia coli. Recombinant Escherichia coli harboring only the decaprenyl diphosphate synthase gene produce 0.21 mg/l of CoQ10, whereas coexpressed Escherichia coli with decaprenyl diphosphate synthase and dxs genes produce 0.37 mg/l of CoQ10
additional information
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the dxs11 gene is transformed into Agrobacterium tumefaciens KCCM 10413, and the resulting recombinant, Agrobacterium tumefaciens pGX11, shows higher UbiQ10 production (502.4 mg/l) and content (8.3 mg/g DCW) than Agrobacterium tumefaciens KCCM 10413, by 21.9 and 23.9%, respectively
additional information
the dxs11 gene is transformed into Agrobacterium tumefaciens KCCM 10413, and the resulting recombinant, Agrobacterium tumefaciens pGX11, shows higher UbiQ10 production (502.4 mg/l) and content (8.3 mg/g DCW) than Agrobacterium tumefaciens KCCM 10413, by 21.9 and 23.9%, respectively
additional information
overexpression of the Arabidopsis thaliana enzyme in transgenic Lavandula latifolia plants leads to increased production of essential oils in the transgenic plants, overview
additional information
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heterologous expression in Morinda citrifolia increases anthraquinones production by about 24%. Overexpression also results in increased levels of mRNA transcripts and enzymic activity compared to the control cell line. In addition, total phenolics and phenylalanine ammonialyase activity are significantly higher in the transgenic line
additional information
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overexpression of the bacterial dxs gene in Solanum tuberosum tubers perturbs the isoprenoid metabolic network, expression analysis of the nine transgenic lines shows that four exhibit the altered regulation phenotype and five show a wild-type phenotype, the tubers with altered regulation phenotype e.g. show earlier apical bud growth with an 56-day-lag period before sprouting with altered phytohormone levels, overview
additional information
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up-regulation of the enzyme through recombinant expression of the Arabidopsis thaliana enzyme enhances production of essential oils in transgenic spike lavender
additional information
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repression of MtDXS2 by RNAi in transgenic hairy roots leads to reduced transcript levels in mycorrhizal roots, and to a concomitant reduction of arbuscular mycorrhizal-induced apocarotenoid accumulation. Data reveal a requirement for DXS2-dependent MEP pathway-based isoprenoid products to sustain mycorrhizal functionality at later stages of the symbiosis. They further validate the concept of a distinct role for DXS2 in secondary metabolism, and offer a novel tool to selectively manipulate the levels of secondary isoprenoids by targeting their precursor supply
additional information
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PADXS1 is a functional protein which is shown by complementation of a DXS-deficient Escherichia coli strain engineered to utilize mevalonate for isoprenoid biosynthesis. In the absence of mevalonate, only cells transformed with a plasmid bearing a functional PADXS1 gene are viable
additional information
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PADXS2A is a functional protein which is shown by complementation of a DXS-deficient Escherichia coli strain engineered to utilize mevalonate for isoprenoid biosynthesis. In the absence of mevalonate, only cells transformed with a plasmid bearing a functional PADXS1 gene are viable
additional information
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PADXS2B is a functional protein which is shown by complementation of a DXS-deficient Escherichia coli strain engineered to utilize mevalonate for isoprenoid biosynthesis. In the absence of mevalonate, only cells transformed with a plasmid bearing a functional PADXS1 gene are viable
