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Information on EC 2.5.1.67 - chrysanthemyl diphosphate synthase and Organism(s) Artemisia spiciformis and UniProt Accession Q7XYS8
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2.5.1.67 chrysanthemyl diphosphate synthaseIUBMB Comments
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.
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Word Map
- 2.5.1.67
-
pyrethrins
-
insecticides
-
monoterpene
-
irregular
-
tanacetum
- flowers
-
farnesyl
-
isoprenoid
- pyrethrum
-
cyclopropanation
- cinerariifolium
-
dmapp
-
monoterpenoids
-
trichomes
-
geranyl
-
isopentenyl
-
emit
- asteraceae
-
lavandulyl
- squalene
- synthesis
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terpene
- gpp
-
head-to-tail
- prenyltransferase
-
artemisia
- tridentata
- phytoene
- plastidial
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trichome-specific
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headspace
The taxonomic range for the selected organisms is: Artemisia spiciformis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cppase, chrysanthemyl diphosphate synthase, fds-5, chrysanthemol synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
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
162875-10-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6 dimethylallyl diphosphate
(R)-lavandulyl diphosphate + (R)-maconelliyl diphosphate + (1R,3R)-chyrsanthemyl diphosphate + 3 diphosphate
-
non-head-to-tail alcohols after incubation of dimethylallyl diphosphate with CPP synthase followed by hydrolysis with alkaline phosphatase
-
?
dimethylallyl diphosphate + isopentenyl diphosphate
diphosphate + geranyl diphosphate
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
-
-
?
isopentenyl diphosphate + dimethylallyl diphosphate
diphosphate + geranyl diphosphate
reaction of EC 2.5.1.10, geranyltranstransferase, a chain elongation
-
-
?
isopentenyl diphosphate + dimethylallyl diphosphate
diphosphate + geranyl diphosphate
-
-
-
?
additional information
?
-
multifunctional enzyme that catalyzes three competing isoprenoid condensation reactions chain elongation, cyclopropanation, and branching, substrate specificity, product analysis, overview
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
-
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
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
-
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
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
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
-
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
a cyclopropanation
an irregular monoterpene product
-
?
2 dimethylallyl diphosphate
diphosphate + lavandulyl 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
-
-
?
2 dimethylallyl diphosphate
diphosphate + lavandulyl diphosphate
reaction of EC 2.5.1.69, lavandulyl diphosphate synthase, a branching reaction
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
-
-
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
-
multistep cyclization cascade, biosynthesic pathway, and family tree of terpenomic diversity, overview
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 dimethylallyl diphosphate
diphosphate + lavandulyl 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
-
-
?
6 dimethylallyl diphosphate
(R)-lavandulyl diphosphate + (R)-maconelliyl diphosphate + (1R,3R)-chyrsanthemyl diphosphate + 3 diphosphate
-
non-head-to-tail alcohols after incubation of dimethylallyl diphosphate with CPP synthase followed by hydrolysis with alkaline phosphatase
-
?
dimethylallyl diphosphate + isopentenyl diphosphate
diphosphate + geranyl diphosphate
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
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
-
multistep cyclization cascade, biosynthesic pathway, and family tree of terpenomic diversity, overview
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
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
-
-
?
2 dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.51
dimethylallyl diphosphate
pH not specified in the publication, temperature not specified in the publication
1.7
isopentenyl diphosphate
pH not specified in the publication, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
dimethylallyl diphosphate
pH not specified in the publication, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
dimethylallyl diphosphate
pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
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
evolution
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CHRDS_ARTSI
394
0
45022
Swiss-Prot
Chloroplast (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
CPPase larger domain structure, modeling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the pre-enzyme contains an N-terminal plastidial targeting sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
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
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
additional information
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
expression of mutant chimeric CPPase-FPPase enzyme in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hemmerlin, A.; Rivera, S.B.; Erickson, H.K.; Poulter, C.D.
Enzymes encoded by the farnesyl diphosphate synthase gene family in the big sagebrush Artemisia tridentata ssp. spiciformis
J. Biol. Chem.
278
32132-32140
2003
Artemisia spiciformis (Q7XYS8)
Christianson, D.W.
Roots of biosynthetic diversity
Science
316
60-61
2007
Artemisia spiciformis
Thulasiram, H.V.; Erickson, H.K.; Poulter, C.D.
A common mechanism for branching, cyclopropanation, and cyclobutanation reactions in the isoprenoid biosynthetic pathway
J. Am. Chem. Soc.
130
1966-1971
2008
Artemisia spiciformis (Q7XYS8)
Lee, J.S.; Pan, J.J.; Ramamoorthy, G.; Poulter, C.D.
Structure-function studies of Artemisia tridentata farnesyl diphosphate synthase and chrysanthemyl diphosphate synthase by site-directed mutagenesis and morphogenesis
J. Am. Chem. Soc.
139
14556-14567
2017
Artemisia spiciformis, Artemisia spiciformis (Q7XYS8)
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