2.5.1.67: chrysanthemyl diphosphate synthase
This is an abbreviated version!
For detailed information about chrysanthemyl diphosphate synthase, go to the full flat file.
Word Map on EC 2.5.1.67
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2.5.1.67
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pyrethrins
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insecticides
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monoterpene
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irregular
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tanacetum
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flowers
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farnesyl
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isoprenoid
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pyrethrum
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cyclopropanation
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cinerariifolium
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dmapp
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monoterpenoids
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trichomes
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geranyl
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isopentenyl
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emit
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asteraceae
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lavandulyl
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squalene
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synthesis
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terpene
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gpp
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head-to-tail
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prenyltransferase
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artemisia
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tridentata
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phytoene
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plastidial
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trichome-specific
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headspace
- 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
-
terpene
- gpp
-
head-to-tail
- prenyltransferase
-
artemisia
- tridentata
- phytoene
- plastidial
-
trichome-specific
-
headspace
Reaction
2 dimethylallyl diphosphate = +
Synonyms
CDS, CDS_CCI2, chrysanthemol synthase, chrysanthemyl diphosphate synthase, CPP, CPP synthase, CPPase, FDS-5
ECTree
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Engineering
Engineering on EC 2.5.1.67 - chrysanthemyl diphosphate synthase
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D243A
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site-directed mutagenesis, the kinetics of the mutant enzyme are similar to those of the wild-type enzyme
E177D
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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
N283D
L7RFF8
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
N283G
L7RFF8
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
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
additional information
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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 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