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
2.5.1.67
-
RECOMMENDED NAME
GeneOntology No.
chrysanthemyl diphosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 dimethylallyl diphosphate = diphosphate + chrysanthemyl diphosphate
show the reaction diagram
-
-
-
-
2 dimethylallyl diphosphate = diphosphate + chrysanthemyl diphosphate
show the reaction diagram
cyclopropanation reaction mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cyclopropanation
Q7XYS8
-
PATHWAY
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CDS_CCI2
E2JFX2
-
chrysanthemyl diphosphate synthase
Q7XYS8
-
CPPase
Q7XYS8
-
FDS-5
Q7XYS8
-
CAS REGISTRY NUMBER
COMMENTARY
162875-10-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
big sagebrush
-
-
Manually annotated by BRENDA team
FDS-5 or ArtCDS; big sagebrush
SwissProt
Manually annotated by BRENDA team
subsp. spiciformis
UniProt
Manually annotated by BRENDA team
i.e. Tanacetum cinerariifolium, dalmatian daisy
-
-
Manually annotated by BRENDA team
i.e. Tanacetum cinerariifolium, dalmatian daisy
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
Q7XYS8
biosynthesis of isoprenoid compounds
physiological function
E2JFX2
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
P0C565, -
-
-
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
Q7XYS8
-
-
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
Q7XYS8
-
-
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
P0C565, -
-
product analysis, chrysanthemyl diphosphate is an irregular monoterpene with a non-head-to-tail or irregular c1'-2-3 linkage between isoprenoid units
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
-
multistep cyclization cascade, biosynthesic pathway, and family tree of terpenomic diversity, overview
-
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
Q7XYS8
a cyclopropanation
an irregular monoterpene product
-
?
dimethylallyl diphosphate
diphosphate + lavandulyl diphosphate
show the reaction diagram
Q7XYS8
reaction of EC 2.5.1.69, lavandulyl diphosphate synthase, a branching reaction
-
-
?
isopentenyl diphosphate + dimethylallyl diphosphate
diphosphate + geranyl diphosphate
show the reaction diagram
Q7XYS8
reaction of EC 2.5.1.10, geranyltranstransferase, a chain elongation
-
-
?
additional information
?
-
P0C565, -
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
-
-
-
additional information
?
-
-
relationships among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway in wild-type and mutant cells, reaction mechanisms, detailed overview
-
-
-
additional information
?
-
P0C565, -
CPPase seems to be incapable of catalyzing 19-4 chain elongation despite its significant sequence homology to FPPase
-
-
-
additional information
?
-
Q7XYS8
multifunctional enzyme that catalyzes three competing isoprenoid condensation reactions chain elongation, cyclopropanation, and branching, substrate specificity, product analysis, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
P0C565, -
-
-
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
Q7XYS8
-
-
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
-
multistep cyclization cascade, biosynthesic pathway, and family tree of terpenomic diversity, overview
-
-
?
additional information
?
-
P0C565, -
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
-
-
-
additional information
?
-
-
relationships among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway in wild-type and mutant cells, reaction mechanisms, detailed overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
Q7XYS8
required, 2 mM
Mg2+
P0C565, -
required, 1-10 mM, can be substituted by Mn2+, best divalent cation
MgCl2
Q7XYS8
10 mM are included in assay medium
Mn2+
P0C565, -
activates, can substitute for Mg2+, optimal at 1 mM, less effective than Mg2+
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
kinetics, wild-type and mutant enzyme
-
additional information
-
additional information
P0C565, -
steady-stae kinetics, the His6-tag of the recombinant enzyme does not influence the kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.008
-
dimethylallyl diphosphate
P0C565, -
pH 7.5, 30°C, His-tagged or detagged recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00267
-
P0C565, -
purified recombinant enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
Q7XYS8
assay at
7.6
-
Q7XYS8
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
Q7XYS8
pH profile
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
P0C565, -
assay at
30
-
Q7XYS8
assay at
37
-
Q7XYS8
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
E2JFX2
expressed in roots, stems, leaves, buds and flowers
Manually annotated by BRENDA team
E2JFX2
expressed in roots, stems, leaves, buds and flowers
Manually annotated by BRENDA team
E2JFX2
expressed in roots, stems, leaves, buds and flowers
Manually annotated by BRENDA team
E2JFX2
expressed in roots, stems, leaves, buds and flowers
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
66000
-
P0C565, -
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
P0C565, -
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 ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
Q7XYS8
the pre-enzyme contains an N-terminal plastidial targeting sequence
proteolytic modification
P0C565, -
the pre-enzyme contains a putative plastidial targeting sequence
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, purified native enzyme in 30% glycerol for about 72 h with 20% decrease in activity
P0C565, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain XA90 by nickel affinity chromatography to over 95% purity
Q7XYS8
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
P0C565, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q7XYS8
expression of mutant chimeric CPPase-FPPase enzyme in Escherichia coli
-
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
Q7XYS8
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
P0C565, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression is upregulated by abscisic acid, methyl jasmonate and ethrel treatment
E2JFX2
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D243A
-
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
-
site-directed mutagenesis, the kinetics of the mutant enzyme are similar to those of the wild-type enzyme
additional information
-
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