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evolution
Dioscorea zingiberensis DzDXR is highly homologous to other plant DXRs, especially to those in monocotyledons
evolution
phylogenetic analysis, rice DXR is encoded by the single copy gene OsDXR and phylogenetically categorized into plant DXR clade II, which includes the tree plants gingko, yew, and pine, and the Poaceae family plants sorghum (Sorghum bicolor), maize, foxtail millet, and barley (Hordeum vulgare). On the other hand, rice DXR is not categorized into clade I, which includes herbage plants
malfunction
DXR is essential for the survival of the pathogen, and its inhibition leads to the antimalarial action
malfunction
DXR is essential for the survival of the pathogen, and its inhibition leads to the antitubercular action
malfunction
MH018577
increased expression of SaDXR leads to increased contents of sandalwood sesquiterpenoids, such as alpha-santalol and beta-santalol, in the stems of young sandalwood trees
malfunction
overexpression of PtDXR in transgenic poplars improves tolerance to abiotic and biotic stresses. Increased transcript levels of PtDXR alter the 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
malfunction
the overexpression of each OsDXS2 or OsDXR causes no positive effect on the accumulation of either carotenoids or chlorophylls in leaves and seeds, but overexpression of either OsDXS2 or OsDXR affects seed carotenoid metabolism, total carotenoid content is increased by 26% in the PGD1::OsDXS2 lines and decreased by 11% in the PGD1::OsDXR lines, overview. 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
malfunction
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DXR is essential for the survival of the pathogen, and its inhibition leads to the antitubercular action
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malfunction
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DXR is essential for the survival of the pathogen, and its inhibition leads to the antitubercular action
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metabolism
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1-deoxy-D-xylulose-5-phosphate, DXP, reductoisomerase catalyzes the first committed step in the 2-C-methyl-D-erythritol 4-phosphate pathway involving a skeletal rearrangement of DXP via a retroaldol/aldol process followed by reduction by NADPH to yield 2-C-methyl-D-erythritol 4-phosphate
metabolism
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the 1-deoxy-D-xylulose-5-phosphate reductoisomerase is the second enzyme in the nonmevalonate isoprene biosynthesis pathway, catalyzing the reductive isomerization of 1-deoxy-D-xylulose-5-phosphate to 2-methyl-D-erythritol-4-phosphate for making isopentenyl diphosphate and dimethylallyl diphosphate
metabolism
the 1-deoxy-D-xylulose-5-phosphate reductoisomerase is the second enzyme in the nonmevalonate isoprene biosynthesis pathway, catalyzing the reductive isomerization of 1-deoxy-D-xylulose-5-phosphate to 2-methyl-D-erythritol-4-phosphate for making isopentenyl diphosphate and dimethylallyl diphosphate
metabolism
the enzyme catalyzes the second regulation step in the 2-C-methyl-D-erythritol 4-phosphate pathway and the the first committed step of the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid biosynthesis
metabolism
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the enzyme is involved in a parasite-specific, isoprenoid biosynthetic DOXP/MEP pathway
metabolism
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the enzyme is involved in the isoprenoid biosynthetic DOXP/MEP pathway
metabolism
1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) is the first key enzyme in the MEP pathway for terpenoid biosynthesis
metabolism
1-deoxy-D-xylulose 5-phosphate-reductoisomerase (DXR,) is the key enzyme in the plastidic 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway. In contrast to the DzDXR transcription, diosgenin is present predominantly in tubers and in minute quantities in leaves. Because diosgenin is very likely formed mainly in the cytosol of mature leaf cells of Dioscorea zingiberensis and the plastidic IPP and DMAPP produced by the MEP pathway can be transported into the cytosol, the consistently high expression of DzDXR detected in mature leaf of Dioscorea zingiberensis implies that the MEP pathway might play a significant role in diosgenin biosynthesis
metabolism
1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) catalyzes the second step of the nonmevalonate (or MEP) pathway that functions in several organisms and plants for the synthesis of isoprenoids
metabolism
1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) catalyzes the second step of the nonmevalonate (or MEP) pathway that functions in several organisms and plants for the synthesis of isoprenoids
metabolism
1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) catalyzes the second step of the nonmevalonate (or MEP) pathway that functions in several organisms and plants for the synthesis of isoprenoids
metabolism
MH018577
1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) is a rate-limiting enzyme that transforms 1-deoxy-D-xylulose 5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) and controls flux through the MEP pathway. Relationship between SaDXR and the biosynthesis of chlorophylls, carotenoids, and sandalwood-specific sesquiterpenoids, overview
metabolism
1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR), an important enzyme in the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway in plant plastids, provides the basic five-carbon units for isoprenoid biosynthesis. Roles of the MEP pathway in regulating growth, development, and artemisinin biosynthesis of Artemisia annua
metabolism
1-deoxy-D-xylulose-5-phosphate synthase (DXS) and 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) are key enzymes in terpenoid biosynthesis. The first two rate-limiting enzymes in the plastid-located 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway are 1-deoxy-D-xylulose-5-phosphate synthase (DXS) and 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR). The first major step involves DXS-dependent catalysis of pyruvate and D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP). The second step is catalyzed by DXR and generates MEP, followed by several enzymatic reactions to produce precursors of IPP and DMAPP. DXS catalyzes the formation of 1-deoxy-D-xylulose 5-phosphate (DXP) from pyruvate and D-glyceraldehyde-3-phosphate. DXR catalyzes the formation of 2-C-methyl-D-erythritol 4-phosphate (MEP) from DXP
metabolism
induction of DXR expression causes increased thymol and carvacrol production
metabolism
organ-specific differential roles of rice Deoxyxylulose 5-phosphate synthase (DXS) and deoxyxylulose 5-phosphate reductoisomerase (DXR), the first two enzymes of the methylerythritol 4-phosphate (MEP) pathway, in carotenoid metabolism in Oryza sativa leaves and seeds. DXS and DXR are the enzymes that catalyze the first two enzyme steps of the MEP pathway to supply the isoprene building-blocks of carotenoids. Enzyme OsDXS2 functions as a rate-limiting enzyme supplying IPP/DMAPPs to seed carotenoid metabolism, but OsDXR does not in either leaves or seeds. Carotenoid and MEP pathway regulation, overview
metabolism
rate-limiting enzyme in the 2-methyl-D-erythritol-4-phosphate (MEP) terpenoid biosynthetic pathway catalyzing the second step
metabolism
the 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) is the rate-limiting enzyme in the methylerythritol 4-phosphate pathway (MEP) via conversion of 1-deoxy-D-xylulose-5-phosphate (DXP) into MEP
metabolism
the enzyme catalyzes the first comitted step in the methyl erythritol phosphate (MEP) pathway
metabolism
the enzyme catalyzes the first comitted step in the methyl erythritol phosphate (MEP) pathway
metabolism
the enzyme catalyzes the first comitted step in the methyl erythritol phosphate (MEP) pathway
metabolism
the enzyme is involved in the 2-methyl-D-erythritol-4-phosphate (MEP) terpenoid biosynthetic pathway catalyzing the second step, pathway overview
metabolism
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the enzyme is involved in the 2C-methyl-D-erythritol 4-phosphate (MEP) pathway in leaves. The MEP pathway initiates the biosynthesis of highly valuable monoterpene indole alkaloids (MIAs). The MIA biosynthetic pathway shows in leaves a complex compartmentation occuring at both the cellular and subcellular levels, notably for some gene products of the MEP pathway. All MEP pathway genes are coordinately and mainly expressed in internal phloem-associated parenchyma of young leaves, reinforcing the role of this tissue in MIA biosynthesis. A potential role of stromules in enhancing MIA precursor exchange with other cell compartments to favor metabolic fluxes towards the MIA biosynthesis. The MEP pathway produces both isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) through seven enzymatic reactions initiated by the synthesis of 1-deoxy-D-xylulose 5-phosphate (DXP) from pyruvate and glyceraldehyde 3-phosphate. This reaction is catalyzed by DXP synthase (DXS), encoded by a small gene family in higher plants. The DXS isogenes have been clustered into two related gene groups: Clade I-DXS including housekeeping genes and Clade II-DXS including genes associated with plant defense and secondary metabolism. DXP is then sequentially converted into MEP by DXP reductoisomerase (DXR) and into 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol (CDP-ME) following the addition of cytidine triphosphate by CDP-ME synthase (CMS), pathway overview. MEP pathway enzymes are targeted to plastids
metabolism
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the enzyme catalyzes the first comitted step in the methyl erythritol phosphate (MEP) pathway
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metabolism
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the enzyme catalyzes the first comitted step in the methyl erythritol phosphate (MEP) pathway
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metabolism
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the enzyme is involved in the 2-methyl-D-erythritol-4-phosphate (MEP) terpenoid biosynthetic pathway catalyzing the second step, pathway overview
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metabolism
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the enzyme catalyzes the first comitted step in the methyl erythritol phosphate (MEP) pathway
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metabolism
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1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) catalyzes the second step of the nonmevalonate (or MEP) pathway that functions in several organisms and plants for the synthesis of isoprenoids
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metabolism
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the enzyme catalyzes the first comitted step in the methyl erythritol phosphate (MEP) pathway
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metabolism
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1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) catalyzes the second step of the nonmevalonate (or MEP) pathway that functions in several organisms and plants for the synthesis of isoprenoids
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physiological function
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influence on plaunotol biosynthesis
physiological function
Vitis vinifera x Vitis vinifera
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involved in terpenoid metabolism
physiological function
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involved in terpenoid metabolism
physiological function
involved in the 2-C-methyl-D-erythritol 4-phosphate pathway
physiological function
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a dxr gene T-DNA insertion mutant shows albino and dwarf phenotype. The mutant does not bolt, has a significantly reduced number of trichomes and most of the stomata cannot close normally in the leaves. Two transgenic co-suppression lines produce more yellow inflorescences and albino sepals with no trichomes. The transcription levels of genes involved in trichome initiation are strongly affected in the mutants. Exogenous application of gibberellic acid GA3 can partially rescue the dwarf phenotype and the trichome initiation of the insertion mutant, and exogenous application of abscisic acid can rescue the stomata closure defect
physiological function
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1-deoxy-D-xylulose-5-phosphate reductoisomerase in the non-mevalonate isoprene biosynthesis pathway is essential to the organism
physiological function
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in transgenic spike lavender plants (Lavandula latifolia) constitutively expressing the Arabidopsis thaliana DXR gene, a clear correlation between transcript accumulation and monoterpene production cannot be established. The DXR enzyme does not play a crucial role in the synthesis of plastidial monoterpene precursors
physiological function
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1-deoxy-xylulose-5-phosphate isomerase-reductase gene (DXR), catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP), which is the key element for MEP-pathway that supports the main C5 units for the formation of mono and diterpenes. Plastidial MEP pathway is considered as the main important source of precursors for essential plastid isoprenoids
physiological function
DXR is essential for the survival of multiple pathogenic bacteria/parasites
physiological function
DXR is essential for the survival of multiple pathogenic bacteria/parasites, including those that cause tuberculosis and malaria in humans
physiological function
DXR is essential for the survival of multiple pathogenic bacteria/parasites, including those that cause tuberculosis and malaria in humans
physiological function
enzyme OsDXS2 functions as a rate-limiting enzyme supplying IPP/DMAPPs to seed carotenoid metabolism, but OsDXR does not in either leaves or seeds. DXR plays essential roles in the development and survival of plants. No positive effect of OsDXR on carotenoid and chlorophyll metabolism in rice leaves. OsDXR-mediated transcriptional alteration of intrinsic carotenogenetic genes in rice leaves and seeds, overview
physiological function
MH018577
enzyme SaDXR protein may be involved in plastidial isoprenoid biosynthesis in plants
physiological function
in many pathogenic bacteria, the enzymes of the 2-C-methyl-D-erythrirol 4-phosphate (MEP) pathway are involved in the biosynthesis of isopentenyl diphosphate and dimethylallyl diphosphate, the two universal and essential units for the biosynthesis of isoprenoids. The enzyme 1-deoxyxylulose 5-phosphate reductoisomerase (DXR) that catalyzes the transformation of 1-deoxy-D-xylulose 5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) via an isomerization and a NADPH-dependent reduction reaction
physiological function
in many pathogenic bacteria, the enzymes of the 2-C-methyl-D-erythrirol 4-phosphate (MEP) pathway are involved in the biosynthesis of isopentenyl diphosphate and dimethylallyl diphosphate, the two universal and essential units for the biosynthesis of isoprenoids. The enzyme 1-deoxyxylulose 5-phosphate reductoisomerase (DXR) that catalyzes the transformation of 1-deoxy-D-xylulose 5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) via an isomerization and a NADPH-dependent reduction reaction
physiological function
PtDXR encodes a functional protein, and widely participates in plant growth and development, stress physiological process
physiological function
the 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR), an NADPH-dependent reductase, plays a pivotal role in the methylerythritol 4-phosphate pathway (MEP), in the conversion of 1-deoxy-D-xylulose-5-phosphate (DXP) into MEP. Structure-function analysis of DXR and regulatory mechanism, molecular dynamics simulations, overview
physiological function
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in many pathogenic bacteria, the enzymes of the 2-C-methyl-D-erythrirol 4-phosphate (MEP) pathway are involved in the biosynthesis of isopentenyl diphosphate and dimethylallyl diphosphate, the two universal and essential units for the biosynthesis of isoprenoids. The enzyme 1-deoxyxylulose 5-phosphate reductoisomerase (DXR) that catalyzes the transformation of 1-deoxy-D-xylulose 5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) via an isomerization and a NADPH-dependent reduction reaction
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physiological function
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DXR is essential for the survival of multiple pathogenic bacteria/parasites, including those that cause tuberculosis and malaria in humans
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physiological function
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DXR is essential for the survival of multiple pathogenic bacteria/parasites, including those that cause tuberculosis and malaria in humans
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additional information
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role of the nonreacting phosphorylmethyl group in catalysis, overview
additional information
two substrate-binding domains, LPADSEHSAI and NKGLEVIEAHY, locate in its mid-region of the enzyme molecule, which is highly homologous to DXRs from other plants and similar to the DXR from Escherichia coli
additional information
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two substrate-binding domains, LPADSEHSAI and NKGLEVIEAHY, locate in its mid-region of the enzyme molecule, which is highly homologous to DXRs from other plants and similar to the DXR from Escherichia coli
additional information
enzyme active site structure analysis
additional information
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enzyme active site structure analysis
additional information
enzyme CaDXR contains three conserved domain, namely NADPH (GSTGSIGT and LAAGSNV), substrate binding (LPADSEHSAI and NKGLEVIEAHY) and Cys-Ser-(Ala/Met/Val/Thr) cleavage-site domains. Three-dimensional molecular modeling and model validation, and molecular dynamics simulation of modeled DXR, overview
additional information
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enzyme CaDXR contains three conserved domain, namely NADPH (GSTGSIGT and LAAGSNV), substrate binding (LPADSEHSAI and NKGLEVIEAHY) and Cys-Ser-(Ala/Met/Val/Thr) cleavage-site domains. Three-dimensional molecular modeling and model validation, and molecular dynamics simulation of modeled DXR, overview
additional information
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enzyme active site structure analysis
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