2.5.1.10: (2E,6E)-farnesyl diphosphate synthase
This is an abbreviated version!
For detailed information about (2E,6E)-farnesyl diphosphate synthase, go to the full flat file.
Word Map on EC 2.5.1.10
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2.5.1.10
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bisphosphonates
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mevalonate
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isoprenoids
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geranylgeranylation
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nitrogen-containing
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prenylation
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sterol
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zoledronate
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cholesterol
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resorption
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dimethylallyl
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squalene
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osteoclast
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osteoporosis
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alendronate
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risedronate
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prenyltransferases
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sesquiterpene
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terpenoids
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dmapp
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allyl
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hmg-coa
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3-hydroxy-3-methylglutaryl
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monoterpene
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isoprenylation
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pamidronate
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ibandronate
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farnesol
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isoprene
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dolichols
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srebps
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osteoclast-mediated
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annua
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aspartate-rich
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clodronate
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cis-prenyltransferase
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etidronate
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homoallylic
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anti-resorptive
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geranylgeraniol
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aminobisphosphonates
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paget
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phosphomevalonate
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polyprenyl
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drug development
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branch-point
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minodronate
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nonsterol
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amorpha-4,11-diene
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medicine
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phosphoantigens
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molecular biology
- 2.5.1.10
- bisphosphonates
- mevalonate
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isoprenoids
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geranylgeranylation
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nitrogen-containing
-
prenylation
- sterol
- zoledronate
- cholesterol
- resorption
-
dimethylallyl
- squalene
- osteoclast
- osteoporosis
- alendronate
- risedronate
- prenyltransferases
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sesquiterpene
-
terpenoids
-
dmapp
-
allyl
- hmg-coa
-
3-hydroxy-3-methylglutaryl
-
monoterpene
-
isoprenylation
- pamidronate
- ibandronate
- farnesol
- isoprene
- dolichols
-
srebps
-
osteoclast-mediated
- annua
-
aspartate-rich
- clodronate
- cis-prenyltransferase
- etidronate
-
homoallylic
-
anti-resorptive
- geranylgeraniol
-
aminobisphosphonates
-
paget
- phosphomevalonate
-
polyprenyl
- drug development
-
branch-point
- minodronate
-
nonsterol
- amorpha-4,11-diene
- medicine
-
phosphoantigens
- molecular biology
Reaction
Synonyms
At4g36810, bifunctional farnesyl/geranylgeranyl diphosphate synthase, E-farnesyl diphosphate synthase, E-FPP synthase, ERG20, farnesyl diphosphate synthase, farnesyl diphosphate synthase 1, farnesyl diphosphate synthase 2, farnesyl pyrophosphate synthase, farnesyl pyrophosphate synthetase, farnesyl-diphosphate synthase, farnesylpyrophosphate synthetase, FDPSase, FDS, FPP synthase, FPP-synthase, FPPase, FPPS, FPPS/GGPPS, FPPS1, FPPS2, FPPS3, FPS, Fps1, FPS2, geranyl transferase I, geranyltranstransferase, GGPPS11, hFPPS, HpGGPPS, IspA, LS1, MpFPPS1, MpFPPS2, omega,E,E-farnesyl diphosphate synthase, omega,E,E-FPP, PA4043, PcIDS1, prenyltransferase, type I farnesyl diphosphate synthase
ECTree
2.5.1.10 (2E,6E)-farnesyl diphosphate synthaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.5.1.10 - (2E,6E)-farnesyl diphosphate synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L110W
about 50% decrease in reaction rate, increase in production of geranyl diphosphate
C73F
I84F
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7.2% of wild-type activity with dimethylallyl diphosphate
S82F
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produces exclusively geranyl diphosphate, i.e. the mutant enzyme has changed from a farnesyl diphosphate synthase to a geranyl diphosphate synthase
Y81D
Y81S
T164F
T164W
T164Y
s228T
inhibition of the bifunctional farnesyl/geranylgeranyl diphosphate synthase by MMV019313, but not bisphosphonates, is disrupted in an S228T variant
K266I
R120G
R121G
A99G
mutant enzyme shows a significant increase in the total concentration of isoprene: 2.4times compared to the wild-type strain. No detection of geranyl diphosphate
A99H
A99K
A99P
mutant enzyme shows a significant increase in the total concentration of isoprene: 6.0times compared to the wild-type strain. The mutant enzyme shows a significant accumulation of isoprene phosphate particularly of isopentenyl diphosphate and/or dimethylallyl diphosphate, which are not detected in the wild-type strain. 1.5fold increase in geranyl diphosphate concentration compared to wild-type enzyme
A99Q
A99R
A99T
A99V
mutant enzyme behaves similarly to the wild-type strain with respect to the geranyl diphosphate content
A99W
mutant enzyme shows a significant increase in the total concentration of isoprene: 2.1times compared to the wild-type strain. 3fold increase in geranyl diphosphate concentration compared to wild-type enzyme
A99Y
K254A/K197G
the mutations result in a loss of enzyme activity and a lethal phenotype
K254E/K197G
the mutations result in a loss of enzyme activity and a lethal phenotype
A99Q
A99T
S50L
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mutant enzyme produces prenyl diphosphates with the same chain lengths as the wild-type enzyme does. 1.3-1.4fold decrease in ratio of Vmax to Km-value for dimethylallyl diphosphate and isopentenyl 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
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
C73F
thermostability of the mutant enzyme C73F is lower than that of the wild-type enzyme, but higher when compared with human enzyme
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
Y81D
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mutant yields higher condensation products than wild-type
Y81S
the mutant catalyzes the reaction between 8-tetrahydropyran-2-yloxygeranyl diphosphate and isopentenyl diphosphate, producing 12-tetrahydropyran-2-yloxyfarnesyl diphosphate with a yield of 12.3%. The mutant catalyzes the reaction between 8-acetoxygeranyl diphosphate with isopentenyl diphosphate, producing 12-acetoxyfarnesyl diphosphate and 16-acetoxygeranylgeranyl diphosphate with respective yields of 55.3% and 1.7%
Y81S
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the mutant catalyzes the reaction between 8-tetrahydropyran-2-yloxygeranyl diphosphate and isopentenyl diphosphate, producing 12-tetrahydropyran-2-yloxyfarnesyl diphosphate with a yield of 12.3%. The mutant catalyzes the reaction between 8-acetoxygeranyl diphosphate with isopentenyl diphosphate, producing 12-acetoxyfarnesyl diphosphate and 16-acetoxygeranylgeranyl diphosphate with respective yields of 55.3% and 1.7%
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T164F
mutation completely abolishes the activity of the enzyme. No significant thermal shift between the wild-type enzyme and the mutants, indicating that the single-point mutations do not disrupt the folding or stability of the enzyme
T164W
mutation completely abolishes the activity of the enzyme. No significant thermal shift between the wild-type enzyme and the mutants, indicating that the single-point mutations do not disrupt the folding or stability of the enzyme
T164Y
mutation displays dual product specificity and produces a mixture geranyl diphosphate and farnesyl diphosphate as final products, with an activity for farnesyl diphosphate synthesis that is lower than that of the wild-type enzyme
T164Y
mutation displays dual product specificity and produces a mixture geranyl diphosphate and farnesyl diphosphate as final products, with an activity for farnesyl diphosphate synthesis that is lower than that of the wild-type enzyme. No significant thermal shift between the wild-type enzyme and the mutants, indicating that the single-point mutations do not disrupt the folding or stability of the enzyme
K266I
the mutation abolishes the activities of isoform FPPS1
K266I
the mutation abolishes the activities of isoform FPPS2
R120G
the mutation abolishes the activities of isoform FPPS1
R120G
the mutation abolishes the activities of isoform FPPS2
R121G
the mutation abolishes the activities of isoform FPPS1
R121G
the mutation abolishes the activities of isoform FPPS2
A99H
the strain carrying the variant shows significant differences on geranyl diphosphate concentrations and specific growth rate
A99H
variant shows significant difference on geranyl diphosphate concentrations and specific growth rate
A99K
the strain carrying the mutant enzyme accumulates high amounts of dimethylallyl diphosphate-isopentenyl diphosphate, with a decrease in geranyl diphosphate and farnesyl diphosphate
A99Q
mutant enzyme shows a significant increase in the total concentration of isoprene: 8.0times compared to the wild-type strain. The mutant enzyme shows a significant accumulation of isoprene phosphate particularly of isopentenyl diphosphate and/or dimethylallyl diphosphate, which are not detected in the wild-type strain. No detection of geranyl diphosphate
A99Q
the strain carrying the mutant enzyme accumulates high amounts of dimethylallyl diphosphate-isopentenyl diphosphate, with a decrease in geranyl diphosphate and farnesyl diphosphate
A99R
the strain carrying the variant shows significant differences on geranyl diphosphate concentrations and specific growth rate
A99R
variant shows significant difference on geranyl diphosphate concentrations and specific growth rate
A99T
mutant enzyme behaves similarly to the wild-type strain with respect to the geranyl diphosphate content
A99T
the mutant produces unquantifiable amounts of farnesyl diphosphate and no effect on geranyl diphosphate production is observed
A99T
the strain carrying the variant produces unquantifiable amounts of farnesyl diphosphate and no effect on geranyl diphosphate production is observed
A99Y
mutant enzyme shows a significant accumulation of isoprene phosphate particularly of isopentenyl diphosphate and/or dimethylallyl diphosphate, which are not detected in the wild-type strain
A99Y
mutant enzyme shows a significant increase in the total concentration of isoprene: 3.1times compared to the wild-type strain. The mutant enzyme shows a significant accumulation of isoprene phosphate particularly of isopentenyl diphosphate and/or dimethylallyl diphosphate, which are not detected in the wild-type strain. No detection of geranyl diphosphate
A99Y
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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mutant enzyme shows a significant increase in the total concentration of isoprene: 8.0times compared to the wild-type strain. The mutant enzyme shows a significant accumulation of isoprene phosphate particularly of isopentenyl diphosphate and/or dimethylallyl diphosphate, which are not detected in the wild-type strain. No detection of geranyl diphosphate
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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
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A99T
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mutant enzyme behaves similarly to the wild-type strain with respect to the geranyl diphosphate content
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A99T
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the mutant produces unquantifiable amounts of farnesyl diphosphate and no effect on geranyl diphosphate production is observed
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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
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