Information on EC 2.5.1.67 - chrysanthemyl diphosphate synthase

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The expected taxonomic range for this enzyme is: Anthemideae

EC NUMBER
COMMENTARY hide
2.5.1.67
-
RECOMMENDED NAME
GeneOntology No.
chrysanthemyl diphosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 dimethylallyl diphosphate = diphosphate + chrysanthemyl diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclopropanation
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyrethrin I biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (chrysanthemyl-diphosphate-forming)
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.
CAS REGISTRY NUMBER
COMMENTARY hide
162875-10-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. spiciformis
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6 dimethylallyl diphosphate
(R)-lavandulyl diphosphate + (R)-maconelliyl diphosphate + (1R,3R)-chyrsanthemyl diphosphate + 3 diphosphate
show the reaction diagram
-
non-head-to-tail alcohols after incubation of dimethylallyl diphosphate with CPP synthase followed by hydrolysis with alkaline phosphatase
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
dimethylallyl diphosphate
diphosphate + lavandulyl diphosphate
show the reaction diagram
reaction of EC 2.5.1.69, lavandulyl diphosphate synthase, a branching reaction
-
-
?
isopentenyl diphosphate + dimethylallyl diphosphate
diphosphate + geranyl diphosphate
show the reaction diagram
reaction of EC 2.5.1.10, geranyltranstransferase, a chain elongation
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6 dimethylallyl diphosphate
(R)-lavandulyl diphosphate + (R)-maconelliyl diphosphate + (1R,3R)-chyrsanthemyl diphosphate + 3 diphosphate
show the reaction diagram
Q7XYS8
-
non-head-to-tail alcohols after incubation of dimethylallyl diphosphate with CPP synthase followed by hydrolysis with alkaline phosphatase
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgCl2
10 mM are included in assay medium
Mn2+
activates, can substitute for Mg2+, optimal at 1 mM, less effective than Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
dimethylallyl diphosphate
Tanacetum cinerariifolium
P0C565
pH 7.5, 30°C, His-tagged or detagged recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00267
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expressed in roots, stems, leaves, buds and flowers
Manually annotated by BRENDA team
expressed in roots, stems, leaves, buds and flowers
Manually annotated by BRENDA team
expressed in roots, stems, leaves, buds and flowers
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 45358, pre-protein, sequence calculation, 1 * 41000, recombinant enzyme, SDS-PAGE, 1 * 41200, recombinant enzyme, analytical sedimentation equilibrium ultracentrifugation
additional information
-
CPPase larger domain structure, modeling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified native enzyme in 30% glycerol for about 72 h with 20% decrease in activity
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
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain XA90 by nickel affinity chromatography to over 95% purity
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
expression of mutant chimeric CPPase-FPPase enzyme in Escherichia coli
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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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is upregulated by abscisic acid, methyl jasmonate and ethrel treatment
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D243A
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site-directed mutagenesis, the kinetics of the mutant enzyme are similar to those of the wild-type enzyme
E177D
-
site-directed mutagenesis, the kinetics of the mutant enzyme are similar to those of the wild-type enzyme
M98I
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site-directed mutagenesis, the kinetics of the mutant enzyme are similar to those of the wild-type enzyme
additional information
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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