2.5.1.1: dimethylallyltranstransferase
This is an abbreviated version!
For detailed information about dimethylallyltranstransferase, go to the full flat file.
Word Map on EC 2.5.1.1
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2.5.1.1
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farnesyl
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monoterpene
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prenyltransferases
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terpenoids
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ggpps
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prenylation
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geraniol
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aspartate-rich
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dmapp
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tryptophan-containing
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myrcene
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carotenogenic
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1-deoxy-d-xylulose-5-phosphate
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uredovora
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neosartorya
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spearmint
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oleoresin
- 2.5.1.1
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farnesyl
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monoterpene
- prenyltransferases
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terpenoids
- ggpps
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prenylation
- geraniol
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aspartate-rich
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dmapp
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tryptophan-containing
- myrcene
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carotenogenic
- 1-deoxy-d-xylulose-5-phosphate
- uredovora
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neosartorya
- spearmint
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oleoresin
Reaction
Synonyms
(E)-geranyl diphosphate synthase, AnaPT, At4g36810, dimethylallyl transferase, ERG20, farnesyl diphosphate synthase, FgaPT2, FPPase, FPPS, FPPS2, geranyl diphosphate synthase, geranyl pyrophosphate synthase, geranylgeranyl pyrophosphate synthase, GGPPS11, GPP (C5) synthase, GPP synthase, GPP/FPP synthase, GPPS, HpGGPPS, IDS, IDS1, IDS2, IdsA, isoprenyl diphosphate synthase, PcIDS1, Rv0989c
ECTree
2.5.1.1 dimethylallyltranstransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.5.1.1 - dimethylallyltranstransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L110W
about 50% decrease in reaction rate, increase in production of geranyl diphosphate
Y81D
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mutant yields higher condensation products than wild-type
F239A
the IC50 of CA28a against the F239A mutant enzyme is about 500% larger than against wild type protein
N59A
CA28a exhibits the same IC50 against the N59A mutant enzyme ass against wild type protein
G257D/P174C
little effect on reactionrate, no effect on product composition
L180F
little effect on reactionrate, product composition is about 98% geranyldiphosphate, 12% geranygeranyl diphosphate
L180F/P174C
little effect on reactionrate, product composition is about 98% geranyldiphosphate, 12% geranygeranyl diphosphate
M165Y
little effect on reactionrate, product composition is about 90% geranyldiphosphate, 10% farnesyl diphosphate
M175I
little effect on reactionrate, product composition is about 95% geranyldiphosphate, 3% farnesyl diphosphate, 25% geranygeranyl diphosphate
M175I/P174C
little effect on reactionrate, single product is geranyldiphosphate
M175I/P174S
little effect on reactionrate, no effect on product composition
A99H
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the strain carrying the variant shows significant differences on geranyl diphosphate concentrations and specific growth rate
A99K
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the strain carrying the mutant enzyme accumulates high amounts of dimethylallyl diphosphate-isopentenyl diphosphate, with a decrease in geranyl diphosphate and farnesyl diphosphate
A99Q
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the strain carrying the mutant enzyme accumulates high amounts of dimethylallyl diphosphate-isopentenyl diphosphate, with a decrease in geranyl diphosphate and farnesyl diphosphate
A99R
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the strain carrying the variant shows significant differences on geranyl diphosphate concentrations and specific growth rate
A99T
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the strain carrying the variant produces unquantifiable amounts of farnesyl diphosphate and no effect on geranyl diphosphate production is observed
A99Y
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the strain carrying the mutant enzyme accumulates high amounts of dimethylallyl diphosphate-isopentenyl diphosphate, with a decrease in geranyl diphosphate and farnesyl diphosphate
Y81D
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contrary to wild-type, reaction of (Z)-ethynyldimethylallyl diphosphate plus isopentenyl diphosphate yields a mixture of products ethynylgeranyl, ethynylfarnesyl, and ethynylgeranylgeranyl diphosphates
additional information
additional information
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Artemisia tridentata ssp. spiciformis farnesyl diphosphate synthase (FPPase) and chrysanthemyl diphosphate synthase (CPPase) are closely related proteins. Farnesyl diphosphate synthase catalyzes the chain elongation of dimethylallyl diphosphate to farnesyl diphosphate by sequential addition of two molecules of isopentenyl diphosphate, while chrysanthemyl diphosphate synthase catalyzes chain elongation of dimethylallyl diphosphate to geranyl diphosphate along with condensation of two molecules of dimethylallyl diphosphate to give irregular isoprenoid carbon skeletons with cyclopropane, branched, and cyclobutane structures. Stepwise replacement of the helices and loops surrounding the active site of farnesyl diphosphate synthase by the corresponding regions from chrysanthemyl diphosphate synthase results in the gradual metamorphosis of the selective efficient chain elongation enzyme to a promiscuous relative that inefficiently catalyzes chain elongation and cyclopropanation/branching/cyclobutanation reactions. The initial replacements shift the preference for synthesis of farnesyl diphosphate to geranyl diphosphate, accompanied by a moderate loss in catalytic efficiency. Formation of irregular products only becomes competitive with chain elongation upon replacement of helix VIII
additional information
Artemisia tridentata ssp. spiciformis farnesyl diphosphate synthase (FPPase) and chrysanthemyl diphosphate synthase (CPPase) are closely related proteins. Farnesyl diphosphate synthase catalyzes the chain elongation of dimethylallyl diphosphate to farnesyl diphosphate by sequential addition of two molecules of isopentenyl diphosphate, while chrysanthemyl diphosphate synthase catalyzes chain elongation of dimethylallyl diphosphate to geranyl diphosphate along with condensation of two molecules of dimethylallyl diphosphate to give irregular isoprenoid carbon skeletons with cyclopropane, branched, and cyclobutane structures. Stepwise replacement of the helices and loops surrounding the active site of farnesyl diphosphate synthase by the corresponding regions from chrysanthemyl diphosphate synthase results in the gradual metamorphosis of the selective efficient chain elongation enzyme to a promiscuous relative that inefficiently catalyzes chain elongation and cyclopropanation/branching/cyclobutanation reactions. The initial replacements shift the preference for synthesis of farnesyl diphosphate to geranyl diphosphate, accompanied by a moderate loss in catalytic efficiency. Formation of irregular products only becomes competitive with chain elongation upon replacement of helix VIII
