Requires a divalent metal ion for activity, with Mg2+ being better than Mn2+ . Chrysanthemyl diphosphate is a monoterpene with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. The mechanism of its formation is similar to that of the early steps of {terp/squalphyto::squalene and phytoene biosynthesis}. Chrysanthemyl diphosphate is the precursor of chrysanthemic acid, the acid half of the pyrethroid insecticides found in chrysanthemums.
Requires a divalent metal ion for activity, with Mg2+ being better than Mn2+ [1]. Chrysanthemyl diphosphate is a monoterpene with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. The mechanism of its formation is similar to that of the early steps of {terp/squalphyto::squalene and phytoene biosynthesis}. Chrysanthemyl diphosphate is the precursor of chrysanthemic acid, the acid half of the pyrethroid insecticides found in chrysanthemums.
reaction of EC 2.5.1.1, chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP
chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP
reaction of EC 2.5.1.69, chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP
irregular monoterpenes are common in Chrysanthemum cinerariaefolium and related members of the asteraceae family, CPP is an intermediate in the biosynthesis of the pyrethrin ester insecticides
irregular monoterpenes are common in Chrysanthemum cinerariaefolium and related members of the asteraceae family, CPP is an intermediate in the biosynthesis of the pyrethrin ester insecticides
relationships among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway in wild-type and mutant cells, reaction mechanisms, detailed overview
chrysanthemyl diphosphate synthase operates in planta as a bifunctional enzyme with chrysanthemol synthase activity. The NDXXD catalytic motif of CDS, under the lower substrate conditions prevalent in plants, also catalyzes the next step, converting CPP into chrysanthemol by hydrolyzing the diphosphate moiety. For the chrysanthemol synthase activity, dimethylallyl diphosphate competes with chrysanthemyl diphosphate as substrate
chrysanthemyl diphosphate synthase operates in planta as a bifunctional enzyme with chrysanthemol synthase activity. The enzyme also catalyzes the next step, converting chrysanthemyl diphosphate into chrysanthemol by hydrolyzing the diphosphate moiety
The enzyme shows activity to produce diphosphates (chrysanthemyl diphosphate and lavandulyl diphosphate) and terpene alcohols (chrysanthemol and lavandulol) from dimethylallyl diphosphate
reaction of EC 2.5.1.69, chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP
reaction of EC 2.5.1.1, chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP
chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP
irregular monoterpenes are common in Chrysanthemum cinerariaefolium and related members of the asteraceae family, CPP is an intermediate in the biosynthesis of the pyrethrin ester insecticides
irregular monoterpenes are common in Chrysanthemum cinerariaefolium and related members of the asteraceae family, CPP is an intermediate in the biosynthesis of the pyrethrin ester insecticides
relationships among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway in wild-type and mutant cells, reaction mechanisms, detailed overview
chrysanthemyl diphosphate synthase operates in planta as a bifunctional enzyme with chrysanthemol synthase activity. The NDXXD catalytic motif of CDS, under the lower substrate conditions prevalent in plants, also catalyzes the next step, converting CPP into chrysanthemol by hydrolyzing the diphosphate moiety. For the chrysanthemol synthase activity, dimethylallyl diphosphate competes with chrysanthemyl diphosphate as substrate
DMAPP, causes significant substrate inhibition at elevated concentrations for chrysanthemol synthesis, increase of DMAPP concentration leads to a decrease of chrysanthemol but a strong further increase of chrysanthemyl diphosphate production
Artemisia tridentata chrysanthemyl diphosphate synthase is an example of an enzyme that has evolved recently from a highly specialized parent. The origins of farnesyl diphosphate synthase date back to the very beginning of cellular life, and the enzyme has perfected its ability to catalyze chain-elongation. In contrast, Artemisia tridentata chrysanthemyl diphosphate synthase has recently evolved from Artemisia tridentata diphosphate synthase, presumably by gene duplication and random mutagenesis but is still a promiscuous inefficient catalyst in comparison with farnesyl diphosphate synthase
overexpression of gene in micro-tom tomato results in dwarf phenotypes characterized with infertile flowers and seedless fruits. Overexpression alters the production of endogenous secondary metabolites
chrysanthemyl diphosphate synthase is the first pathway-specific enzyme in the biosynthesis of pyrethrins, the most widely used plant-derived pesticide. The enzyme shows activity to produce diphosphates (chrysanthemyl diphosphate and lavandulyl diphosphate) and terpene alcohols (chrysanthemol and lavandulol) from dimethylallyl diphosphate
overexpression of the CHS gene in Chrysanthemum morifoliumresults in both the emission of volatile chrysanthemol (ca. 47 pmol/h/g FW) and accumulation of chrysanthemyl-6-O-malonyl-beta-D-glucopyranoside (ca. 1.1 mM), with no detrimental phenotypic effects. Both components show independent effects against the cotton aphid (Aphis gossypii). The CHS expressing plants significantly reduce aphid reproduction, consistent with disturbance of aphid probing activities on these plants
site-directed mutagenesis, replacing the asparagine with either aspartate or glycine in the aspartate-rich motif abolishes the enzyme's terpene synthase and prenyltransferase activities
site-directed mutagenesis, replacing the asparagine with either aspartate or glycine in the aspartate-rich motif abolishes the enzyme's terpene synthase and prenyltransferase activities
construction of mutant enzymes as CPPase-FPPase chimeras with the larger domains of CPPase substituted for FPPase in the Artemisia tridentata enzyme, the CPPase-FPPase chimeras are biosynthetically more promiscuous than either native CPPase or FPPase as a result of a reshaped template for substrate binding, which permits alternative trajectories for intermolecular carbon-carbon bond formation, overview
construction of chimera between chrysanthemyl diphosphate synthase CPPase and farnesyl diphosphate synthase FPPase, EC 2.5.1.10 by sequentially replacing the loops and helices of the six-helix bundle from one enzyme with those from the other. Chain elongation is the dominant activity during the N-terminal to C-terminal metamorphosis of FPPase to CPPase, with product selectivity gradually switching from FPP to GPP, until replacement of the final alpha-helix, where upon cyclopropanation and branching activity compete with chain elongation. During the metamorphosis of CPPase to FPPase, cyclopropanation and branching activities are lost upon replacement of the first helix in the six-helix bundle. Mutations of active site residues in CPPase to the corresponding amino acids in FPPase enhance chain-elongation activity, while similar mutations in the active site of FPPase fail to significantly promote formation of significant amounts of irregular monoterpenes
construction of chimera between chrysanthemyl diphosphate synthase CPPase and farnesyl diphosphate synthase FPPase, EC 2.5.1.10 by sequentially replacing the loops and helices of the six-helix bundle from one enzyme with those from the other. Chain elongation is the dominant activity during the N-terminal to C-terminal metamorphosis of FPPase to CPPase, with product selectivity gradually switching from FPP to GPP, until replacement of the final alpha-helix, where upon cyclopropanation and branching activity compete with chain elongation. During the metamorphosis of CPPase to FPPase, cyclopropanation and branching activities are lost upon replacement of the first helix in the six-helix bundle. Mutations of active site residues in CPPase to the corresponding amino acids in FPPase enhance chain-elongation activity, while similar mutations in the active site of FPPase fail to significantly promote formation of significant amounts of irregular monoterpenes
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from immature flowers by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, followed by another step of anion chromatography and hydroxylapatite chromatography to apparent homogeneity, recombinant N-terminally His6-tagged enzyme from Escherichia coli strain XA90 by ammonium sulfate fractionation and nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a c98f chimera is constructed by replacing the first 98 residues in Artemisia tridentata subsp. spiciformis farnesyl diphosphate synthase with the corresponding sequence from chrysanthemyl diphosphate synthase, the enzymes are cloned in Escherichia coli hosts
gene CDS, dNA and amino acid sequence determination and analysis, sequence comparisons, recombinant CDS overexpression under the control of chrysanthemum RbcS1 promoter in transgenic Nicotiana tabacum cv. Samsun plants, in leaf chloroplasts, using Agrobacterium tumefaciens strain AGL-0 transfection method, the expression leads to emittation of chrysanthemol. Recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(AI)
gene FDS-5, cDNA library screening, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression of N-terminally His6-tagged enzyme in Escherichia coli strain XA90, expression of the fusion FDS-5 transit peptide-GFP protein in Nicotiana tabacum cv. xanthi cells with plastidial localization
phage lambda cDNA library screening, DNA and amino acid sequence determination and analysis, functional overexpression of N-terminally His6-tagged enzyme in Escherichia coli strain XA90
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a blend of volatiles (Z)-3-hexenal, (E)-2-hexenal, (Z)-3-hexen-1-ol, (Z)-3-hexenyl acetate and (E)-beta-farnesene, emitted from mechanically wounded leaves, induces the enzyme, effects on several biosynthetic gene expressions in unwounded seedlings of Tanacetum cinerariifolium. The treatment results in enhanced chrysanthemyl diphosphate synthase (CDS), chrysanthemic acid synthase (CAS), GDSL lipase (TcGLIP) and acyl-coenzyme A oxidase 1 (ACX1) gene expressions, overview
construction of the trans-chrysanthemic acid biosynthetic pathway in tomato fruits by expressing the chrysanthemyl diphosphate synthase gene, as well as an alcohol dehydrogenease (ADH) gene and aldehyde dehydrogenase (ALDH) gene from a wild tomato species, all under the control of the PG promoter. Trangenic tomato fruits show a concentration of trans-chrysanthemic acid that is about 1.7fold higher (by weight) than the levels of lycopene present in non-transgenic fruit, the level of lycopene in the transgenic plants is reduced by 68%. Ninety seven percent of the diverted DMAPP is converted to trans-chrysanthemic acid, but 62% of this acid is further glycosylated
transient coexpression of CDS with ADH2 which encodes an enzyme that oxidizes trans-chrysanthemol to trans-chrysanthemal, and ALDH1 which encodes an enzyme that oxidizes trans-chrysanthemal into trans-chrysanthemic acid, in Nicotiana benthamiana leaves results in the production of trans-chrysanthemic acid as well as several other side products. The majority (58%) of trans-chrysanthemic acid is glycosylated or otherwise modified
Chrysanthemyl diphosphate synthase. The relationship among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway
Chrysanthemyl diphosphate synthase: isolation of the gene and characterization of the recombinant non-head-to-tail monoterpene synthase from Chrysanthemum cinerariaefolium
Structure-function studies of Artemisia tridentata farnesyl diphosphate synthase and chrysanthemyl diphosphate synthase by site-directed mutagenesis and morphogenesis
Xu, H.; Moghe, G.D.; Wiegert-Rininger, K.; Schilmiller, A.L.; Barry, C.S.; Last, R.L.; Pichersky, E.
Coexpression analysis identifies two oxidoreductases involved in the biosynthesis of the monoterpene acid moiety of natural pyrethrin insecticides in Tanacetum cinerariifolium