2.5.1.29: geranylgeranyl diphosphate synthase
This is an abbreviated version!
For detailed information about geranylgeranyl diphosphate synthase, go to the full flat file.
Word Map on EC 2.5.1.29
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2.5.1.29
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geranylgeranylation
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isoprenoids
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carotenoid
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bisphosphonates
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prenylation
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mevalonate
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dimethylallyl
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phytoene
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prenyltransferases
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diterpene
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allyl
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diterpenoids
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isoprenylation
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lycopene
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taxus
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uredovora
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aspartate-rich
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synthesis
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kaurene
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drug development
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diagnostics
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fujikuroi
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taxadiene
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medicine
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agriculture
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pharmacology
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nutrition
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20-carbon
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dmapp
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carotenogenesis
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carotenogenic
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biotechnology
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copalyl
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food industry
- 2.5.1.29
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geranylgeranylation
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isoprenoids
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carotenoid
- bisphosphonates
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prenylation
- mevalonate
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dimethylallyl
- phytoene
- prenyltransferases
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diterpene
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allyl
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diterpenoids
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isoprenylation
- lycopene
- taxus
- uredovora
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aspartate-rich
- synthesis
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kaurene
- drug development
- diagnostics
- fujikuroi
- taxadiene
- medicine
- agriculture
- pharmacology
- nutrition
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20-carbon
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dmapp
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carotenogenesis
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carotenogenic
- biotechnology
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copalyl
- food industry
Reaction
Synonyms
At4g36810, bifunctional farnesyl/geranylgeranyl diphosphate synthase, BTS1, CcGGDPS1, CcGGDPS2, CotB1, CrtE, DR1395, EgcrtE, EuFPS1, EuFPS2, farnesyl diphosphate/geranylgeranyl diphosphate synthase, farnesyl-diphosphate/geranylgeranyldiphosphate, farnesyltransferase, FPPS/GGPPS, geranylgeranyl diphosphate synthase, geranylgeranyl diphosphate synthase 1, geranylgeranyl diphosphate synthase 11, geranylgeranyl pyrophosphate synthase, geranylgeranyl pyrophosphate synthase GACE1337, geranylgeranyl pyrophosphate synthase GGPPS1-1, geranylgeranyl pyrophosphate synthase GGPPS1-2, geranylgeranyl pyrophosphate synthetase, geranylgeranyl-PP synthetase, geranylgeranyl-pyrophosphate synthase, GGDP synthase, GGDPS, GGPP synthase, GGPP-S, GGPPase, GGPPS, GGPPS 1, GGPPS 191, GGPPS 2, GGPPS 3, GGPPS 595, GGPPS 727, GGPPS1, GGPPS11, GGPS, Ggps1, GGs1, GgsA, GgsB, GGSP1, gps, HpGGPPS, HsGGPPS, IbGGPS, IdsA, isoprenyl diphosphate synthase, leaf-specific geranylgeranyl pyrophosphate synthase, More, PaxG, PfFPPS, PfGGPPS, Saci_0092, short-chain type-III GGPP, synthetase, geranylgeranyl pyrophosphate, TgFPPS, Tk-IdsA, trans-prenyl diphosphate synthase, type II geranylgeranyl diphosphate synthase, type-III geranylgeranyl pyrophosphate synthase, type-III GGPPS
ECTree
2.5.1.29 geranylgeranyl diphosphate synthaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.5.1.29 - geranylgeranyl diphosphate synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H72A
the mutant enzyme shows less than 5% of the activity as compared to wild-type enzyme
N73A
the mutant enzyme shows less than 5% of the activity as compared to wild-type enzyme
R43A
the mutant enzyme shows less than 5% of the activity as compared to wild-type enzyme
R88A
the mutant enzyme shows less than 5% of the activity as compared to wild-type enzyme
R89A
the mutant enzyme shows less than 5% of the activity as compared to wild-type enzyme
H72A
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the mutant enzyme shows less than 5% of the activity as compared to wild-type enzyme
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N73A
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the mutant enzyme shows less than 5% of the activity as compared to wild-type enzyme
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R43A
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the mutant enzyme shows less than 5% of the activity as compared to wild-type enzyme
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R88A
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the mutant enzyme shows less than 5% of the activity as compared to wild-type enzyme
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R89A
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the mutant enzyme shows less than 5% of the activity as compared to wild-type enzyme
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A89F
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mutant enzyme yields shorter products than the wild-type enzyme. Substrate specificity is almost identical to that of farnesyl diphosphate synthase
A89H
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mutant enzyme yields shorter products than the wild-type enzyme. Substrate specificity is almost identical to that of farnesyl diphosphate synthase
H87A
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activity using geranylgeranyl diphosphate as the substrate is undetectable
L162A/V163A
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altered substrate specificity, hardly accepts dimethylallyl diphosphate as substrate. Yields the products with the same chain-length with those of wild type
G257D/P174C
little effect on reation rate, no effect on product composition
L180F
little effect on reation rate, product composition is about 98% geranyldiphosphate, 12% geranygeranyl diphosphate
L180F/P174C
little effect on reation rate, product composition is about 98% geranyldiphosphate, 12% geranygeranyl diphosphate
M165Y
little effect on reation rate, product composition is about 90% geranyldiphosphate, 10% farnesyl diphosphate
M175I
little effect on reation rate, product composition is about 95% geranyldiphosphate, 3% farnesyl diphosphate, 25% geranygeranyl diphosphate
M175I/P174C
little effect on reation rate, single product is geranyldiphosphate
M175I/P174S
little effect on reation rate, no effect on product composition
s228T
DELTA1-7
29% of wild-type activity. Dimer and monomer formation
F108A
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site-directed mutagenesis, mutant activity, substrate specificity, and product distribution compared to the wild-type enzyme
F108A/H139A
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site-directed mutagenesis, mutant activity, substrate specificity, and product distribution compared to the wild-type enzyme
F96C
site-directed mutagenesis, the mutant shows increased sclareol biosynthesis compared to the wild-type
F96S
site-directed mutagenesis, the mutant shows increased sclareol biosynthesis compared to the wild-type
H139A
H139A/R140A
site-directed mutagenesis, inactive monomeric mutant
L135A/H139A
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site-directed mutagenesis, mutant activity, substrate specificity, and product distribution compared to the wild-type enzyme
L138A
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mutation upstream from the G(Q/E) motif. Mutant forms larger condensation products than wild-type. With farnesyl diphosphate as allylic substrate, mutant produces large amounts of a C25 product
M111A
site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme
M111E
site-directed mutagenesis, the dimeric/monomeric mutant shows altered kinetics compared to the wild-type enzyme
M111F
site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme
N101A
site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme
N101A/N104A
site-directed mutagenesis, the dimeric mutant shows reduced kcat compared to the wild-type
N101A/N104A/Y105A
site-directed mutagenesis, inactive dimeric mutant
N101A/Y105A
site-directed mutagenesis, the dimeric mutant shows reduced kcat compared to the wild-type
N104A
site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme
N104A/Y105A
site-directed mutagenesis, the dimeric mutant shows slightly reduced activity compared to the wild-type
R140A
S71Y
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site-directed mutagenesis, mutant activity, substrate specificity, and product distribution compared to the wild-type enzyme
Y105A
site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme
Y107A
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site-directed mutagenesis, mutant activity, substrate specificity, and product distribution compared to the wild-type enzyme
Y107A/F108A
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site-directed mutagenesis, mutant activity, substrate specificity, and product distribution compared to the wild-type enzyme
Y107A/F108A//L135A/H139A
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site-directed mutagenesis, mutant activity, substrate specificity, and product distribution compared to the wild-type enzyme
Y107A/F108A/H139A
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site-directed mutagenesis, mutant activity, substrate specificity, and product distribution compared to the wild-type enzyme
Y107A/H139A
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site-directed mutagenesis, mutant activity, substrate specificity, and product distribution compared to the wild-type enzyme
Y95A
site-directed mutagenesis, the mutant shows increased sclareol biosynthesis compared to the wild-type
Y95C/F96H
site-directed mutagenesis, the mutant shows increased sclareol biosynthesis compared to the wild-type
Y95L/F96I
site-directed mutagenesis, the mutant shows increased sclareol biosynthesis compared to the wild-type
Y95S/F96H
site-directed mutagenesis, the mutant shows increased sclareol biosynthesis compared to the wild-type
D170E/M171P/I172A/S173M
D170E/M171P/I172A/S173R
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low activity with dimethylallyl diphosphate, approx. 60% of wild-type activity with geranyl diphosphate
D170E/M171P/I172R/S173V
F77G/H114G
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although its activity is approximately 2-5% of the wild-type, this double-mutated enzyme exhibits a detectable activity and a thermostability to resist 15 h of heat treatment at 55°C. C50-prenyl diphosphate is the main long product
I147F
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mutant does not accept farnesyl diphosphate as the allylic substrate, indicating a change in product specificity into that of farnesyl diphosphate synthase
M171P
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low activity with dimethylallyl diphosphate, approx. 50% of wild-type activity with geranyl diphosphate
M171P/I172R
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no activity with dimethylallyl diphosphate, low activity with geranyl diphosphate
M171P/S173V
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very low activity with dimethylallyl diphosphate, approx. 50% of wild-type activity with geranyl diphosphate
S148F
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mutant does not accept farnesyl diphosphate as the allylic substrate, indicating a change in product specificity into that of farnesyl diphosphate synthase
S148H
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mutant does not accept farnesyl diphosphate as the allylic substrate, indicating a change in product specificity into that of farnesyl diphosphate synthase
M87A
mutant enzyme produces the longer C25-geranylfarnesyl pyrophosphate product
M87F
S88Y
V161M
the mutant enzyme, similar amounts of farnesyl diphosphate and geranylgeranyl diphosphate are produced and there is no evidence for formation of geranyl diphosphate
M87A
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mutant enzyme produces the longer C25-geranylfarnesyl pyrophosphate product
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M87F
S88Y
additional information
s228T
inhibition of the bifunctional farnesyl/geranylgeranyl diphosphate synthase by MMV019313, but not bisphosphonates, is disrupted in an S228T variant
s228T
inhibition of then bifunctional farnesyl/geranylgeranyl diphosphate synthase by N-[3-(1-azepanyl)propyl]-5-methyl-4-oxo-4,5-dihydrothieno[3,2-c]quinoline-2-carboxamide (MMV019313), but not bisphosphonates, is disrupted in the S228T variant
s228T
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inhibition of then bifunctional farnesyl/geranylgeranyl diphosphate synthase by N-[3-(1-azepanyl)propyl]-5-methyl-4-oxo-4,5-dihydrothieno[3,2-c]quinoline-2-carboxamide (MMV019313), but not bisphosphonates, is disrupted in the S228T variant
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H139A
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site-directed mutagenesis, mutant activity, substrate specificity, and product distribution compared to the wild-type enzyme
H139A
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mutation upstream from the G(Q/E) motif. Mutant forms larger condensation products than wild-type. With farnesyl diphosphate as allylic substrate, mutant produces large amounts of a C30 product
H139A
site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme
R140A
site-directed mutagenesis, the dimeric mutant shows altered kinetics compared to the wild-type enzyme
D170E/M171P/I172A/S173M
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no activity with dimethylallyl diphosphate, low activity with geranyl diphosphate
D170E/M171P/I172A/S173M
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mutant enzyme shows considerably lower activity toward primer substrates with a short prenyl chain, DMAPP and GPP, than the wild-type enzyme
D170E/M171P/I172R/S173V
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no activity with dimethylallyl diphosphate, low activity with geranyl diphosphate
D170E/M171P/I172R/S173V
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mutant enzyme shows considerably lower activity toward primer substrates with a short prenyl chain, DMAPP and GPP, than the wild-type enzyme. Scarcely accepts DMAPP as an allylic substrate. The mutant enzyme can not catalyze condensation of 3,7,ll-trimethyl-2,6,10,14-heptadecatetraenyl diphosphate with isopentenyl diphosphate. Does not accept short allylic substrates but forms products with the same length as those of the wild-type enzyme
M87F
the mutant enzyme can only generate farnesyl diphosphate, indicating that residues with large side chains obstruct product elongation
S88Y
the mutant enzyme can only generate farnesyl diphosphate, indicating that residues with large side chains obstruct product elongation
M87F
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the mutant enzyme can only generate C15-farnesyl pyrophosphate
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M87F
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the mutant enzyme can only generate farnesyl diphosphate, indicating that residues with large side chains obstruct product elongation
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S88Y
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the mutant enzyme can only generate C15-farnesyl pyrophosphate
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S88Y
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the mutant enzyme can only generate farnesyl diphosphate, indicating that residues with large side chains obstruct product elongation
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additional information
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geranyl phosphate synthase small subunit of Antirrhinum majus forms chimeric geranyl phosphate synthases with geranylgeranyl diphosphate synthase GGPPS1 or GGPPS2 in Nicotiana tabacum. The formation of chimeric GPPS in transgenic plants also results in leaf chlorosis, increased light sensitivity, and dwarfism due to decreased levels of chlorophylls, carotenoids, and gibberellins. Transgenic plants have reduced levels of sesquiterpene emission
additional information
an F2 mapping population is established by crossing ggps1-1 (Col ecotype) with the LER ecotype of Arabidopsis thaliana, analysis of sequence polymorphisms in 209 F2 recombinant lines homozygous for the ggps1-1 variegated phenotype place the mutation in a 63-kb region on chromosome 4 contained on bacterial artificial chromosome AP22. Phenotype analysis of two lines with T-DNA insertions in the coding region of At4g36810 (Salk_015098 and Salk_085914), and mutant ggps1-1 phenotype, detailed overview
additional information
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an F2 mapping population is established by crossing ggps1-1 (Col ecotype) with the LER ecotype of Arabidopsis thaliana, analysis of sequence polymorphisms in 209 F2 recombinant lines homozygous for the ggps1-1 variegated phenotype place the mutation in a 63-kb region on chromosome 4 contained on bacterial artificial chromosome AP22. Phenotype analysis of two lines with T-DNA insertions in the coding region of At4g36810 (Salk_015098 and Salk_085914), and mutant ggps1-1 phenotype, detailed overview
additional information
construction of several GGPPS11 homozygous transgenic lines containing each a single T-DNA insertion that inactivates gene GGPPS11, mutant genotyping, overview
additional information
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construction of several GGPPS11 homozygous transgenic lines containing each a single T-DNA insertion that inactivates gene GGPPS11, mutant genotyping, overview
additional information
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construction of several GGPPS11 homozygous transgenic lines containing each a single T-DNA insertion that inactivates gene GGPPS11, mutant genotyping, overview
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additional information
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an F2 mapping population is established by crossing ggps1-1 (Col ecotype) with the LER ecotype of Arabidopsis thaliana, analysis of sequence polymorphisms in 209 F2 recombinant lines homozygous for the ggps1-1 variegated phenotype place the mutation in a 63-kb region on chromosome 4 contained on bacterial artificial chromosome AP22. Phenotype analysis of two lines with T-DNA insertions in the coding region of At4g36810 (Salk_015098 and Salk_085914), and mutant ggps1-1 phenotype, detailed overview
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additional information
functional completmentation of gene crtE in Escherichia coli
additional information
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combined overexpression of idsA and the IPP isomerase gene idi in the absence of crtE leads to a very high decaprenoxanthin titer
additional information
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generation of gene idsA-deficient Corynebacterium glutamicum cells. Combined overexpression of idsA and the IPP isomerase gene idi in the absence of crtE leads to a very high decaprenoxanthin titer
additional information
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combined overexpression of idsA and the IPP isomerase gene idi in the absence of crtE leads to a very high decaprenoxanthin titer
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additional information
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generation of gene idsA-deficient Corynebacterium glutamicum cells. Combined overexpression of idsA and the IPP isomerase gene idi in the absence of crtE leads to a very high decaprenoxanthin titer
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additional information
transgenic tobacco plants expressing heterologous GGPS from Helianthus annuus show remarkably enhanced growth (an increase in shoot and root biomass and height), early flowering, increased number of seed pods and greater seed yield compared with control or wild-type plants. HaGGPS expression in transgenic tobacco enhances root growth. The gibberellin levels in HaGGPS-transgenic plants are higher than those in control plants, indicating that the observed phenotype may result from increased gibberellin content. No phenotypic defects in the transgenic plants. Enhanced growth in HaGGPS-transgenic Arabidopsis thaliana and Taraxacum brevicorniculatum plants
additional information
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women with 2 deletion alleles of GGPS1 -8188A ins/del (rs3840452) have significantly higher femoral neck bone marrow densitiy at baseline compared with those with one or no deletion allele. The response rate of women with 2 deletion alleles of GGPS1 -8188A ins/del (28.6%) is significantly lower than the rate of women with one or no deletion allele. Women with 2 deletion alleles of GGPS1 -8188A ins/del have 7fold higher risk of non-response to bisphosphonate therapy compared with women with other genotypes in GGPS1 -8188. Other polymorphisms in or GGPS1 are not associated with lumbar spine bone marrow density or femoral neck bon marrow density
additional information
coexpression of both small and large subunits in Escherichia coli yields a heterodimeric enzyme exhibiting altered ratios of GPP and GGPP synthase activities and greatly enhanced catalytic efficiency. The heterodimeric geranyl(geranyl)diphosphate synthase G(G)PPS may be involved in myrcene biosynthesis in hop trichomes. The conserved CxxxC motif, where x can be any hydrophobic amino acid residue, plays a critical role of in physical interactions between the 2 subunits
additional information
coexpression of both small and large subunits in Escherichia coli yields a heterodimeric enzyme exhibiting altered ratios of GPP and GGPP synthase activities and greatly enhanced catalytic efficiency. The heterodimeric geranyl(geranyl)diphosphate synthase G(G)PPS may be involved in myrcene biosynthesis in hop trichomes. The conserved CxxxC motif, where x can be any hydrophobic amino acid residue, plays a critical role of in physical interactions between the 2 subunits
additional information
small subunit alone is inactive. Coexpression of both small and large subunits in Escherichia coli yields a heterodimeric enzyme exhibiting altered ratios of GPP and GGPP synthase activities and greatly enhanced catalytic efficiency. The heterodimeric geranyl(geranyl)diphosphate synthase G(G)PPS may be involved in myrcene biosynthesis in hop trichomes. The conserved CxxxC motif, where x can be any hydrophobic amino acid residue, plays a critical role of in physical interactions between the 2 subunits
additional information
small subunit alone is inactive. Coexpression of both small and large subunits in Escherichia coli yields a heterodimeric enzyme exhibiting altered ratios of GPP and GGPP synthase activities and greatly enhanced catalytic efficiency. The heterodimeric geranyl(geranyl)diphosphate synthase G(G)PPS may be involved in myrcene biosynthesis in hop trichomes. The conserved CxxxC motif, where x can be any hydrophobic amino acid residue, plays a critical role of in physical interactions between the 2 subunits
additional information
expression of the sweetpotato geranylgeranyl pyrophosphate synthase gene IbGGPS in Arabidopsis thaliana increases carotenoid content and enhances osmotic stress tolerance in the transgenic plants. Transgenic seedlings grow significantly longer roots compared to wild-type. Quantitative RT-PCR analysis shows altered expressions of several genes involved in the carotenoid biosynthesis in transgenic plants
additional information
functional expression in Escherichia coli
additional information
inducible lung epithelium-specific GGPS1 knockout mice (SPC-rtTA/TetO-Cre/Ggps1flox/flox) are generated by crossing Ggps1flox/flox mice with SPC-rtTA mice and TetOCre mice. All mice are backcrossed for at least six generations to C57BL/6J strain background and are genotyped by genomic DNA PCR
additional information
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inducible lung epithelium-specific GGPS1 knockout mice (SPC-rtTA/TetO-Cre/Ggps1flox/flox) are generated by crossing Ggps1flox/flox mice with SPC-rtTA mice and TetOCre mice. All mice are backcrossed for at least six generations to C57BL/6J strain background and are genotyped by genomic DNA PCR
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additional information
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isoforms GGPPS2 and GGPPS1 can form functional heterodimers with heterologously expressed geranyl phosphate synthase small subunit of Antirrhinum majus. The formation of chimeric GPPS in transgenic plants also results in leaf chlorosis, increased light sensitivity, and dwarfism due to decreased levels of chlorophylls, carotenoids, and gibberellins. Transgenic plants have reduced levels of sesquiterpene emission
additional information
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functional expression in Escherichia coli. A truncated PaxG mutant lacking the C-terminal tripeptide GRV is unable to complement a DeltapaxG mutant
additional information
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functional expression in Escherichia coli. In the DeltapaxG mutant background ggsA is unable to complement paxilline biosynthesis
additional information
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engineering of Xanthophyllomyces dendrorhous by transforming it with the crtE cDNA to divert metabolite flow from the sterol pathway towards carotenoid biosynthesis. Transformants show increased levels of geranylgeranyl diphosphate synthase leading to higher carotenoid levels including astaxanthin by 8fold
additional information
Phaffia rhodozyma CBS6938, ATCC 96594
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engineering of Xanthophyllomyces dendrorhous by transforming it with the crtE cDNA to divert metabolite flow from the sterol pathway towards carotenoid biosynthesis. Transformants show increased levels of geranylgeranyl diphosphate synthase leading to higher carotenoid levels including astaxanthin by 8fold
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additional information
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the farnesyl-transferring activities of wild-type GGPS, DELTA-4, DELTA-8 and DELTA-12 carboxyterminal deletion mutants are relatively in a ratio of 1.0, 0.84, 0.26 and 0.0015. Each Km value of the four recombinants are estimated to be 0.00071, 0.002, 0.0028 and 0.055 mM for farnesyl diphosphate and to be 0.0029, 0.0051, 0.056 and above 0.1 mM for isopentenyl diphosphate, respectively. Allylic substrate specificities of these recombinants are estimated by quantitative analysis of the products, revealing that DELTA-8 and DELTA-12 mutants lack the ability to accept dimethylallyl and geranyl diphosphates compared to wild-type GGPS and DELTA-4 mutant
additional information
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deletion of the first 9 or 17 amino acids caused the dissociation of dimer into monomer, the DELTA1-17 mutant shows abolished enzyme activity
additional information
efficient diterpene production in yeast by engineering farnesyl diphosphate synthase Erg20p, EC 2.5.1.10, into a geranylgeranyl diphosphate synthase, overview. Several Erg20p mutants support sclareol yield significantly higher than the yield obtained by overexpression of Cistus creticus GGPPS. A single chromosomally integrated copy of the ERG20(F96C) mutant gene is significantly more efficient than overexpression of a heterologous fungal GGPP synthase in redirecting precursor fluxes towards the diterpene branch
additional information
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efficient diterpene production in yeast by engineering farnesyl diphosphate synthase Erg20p, EC 2.5.1.10, into a geranylgeranyl diphosphate synthase, overview. Several Erg20p mutants support sclareol yield significantly higher than the yield obtained by overexpression of Cistus creticus GGPPS. A single chromosomally integrated copy of the ERG20(F96C) mutant gene is significantly more efficient than overexpression of a heterologous fungal GGPP synthase in redirecting precursor fluxes towards the diterpene branch
additional information
isozyme GGPS1 expression is induced in leaves by spider mite Tetranychus urticae feeding and mechanical wounding in wild type tomato but not in the jasmonic acid-response mutant def-1 and the salicylic acid-deficient transgenic NahG line, isozyme GGPS2 is not induced in leaves by spider mite-feeding, wounding, jasmonic acid or methyl salicylate, overview
additional information
isozyme GGPS1 expression is induced in leaves by spider mite Tetranychus urticae feeding and mechanical wounding in wild type tomato but not in the jasmonic acid-response mutant def-1 and the salicylic acid-deficient transgenic NahG line, isozyme GGPS2 is not induced in leaves by spider mite-feeding, wounding, jasmonic acid or methyl salicylate, overview
additional information
isozyme GGPS1 expression is induced in leaves by spider mite Tetranychus urticae feeding and mechanical wounding in wild type tomato but not in the jasmonic acid-response mutant def-1 and the salicylic acid-deficient transgenic NahG line, overview
additional information
isozyme GGPS1 expression is induced in leaves by spider mite Tetranychus urticae feeding and mechanical wounding in wild type tomato but not in the jasmonic acid-response mutant def-1 and the salicylic acid-deficient transgenic NahG line, overview
additional information
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the sequence between position 77 and position 86 of geranylgeranyl diphosphate synthase has been replaced with the corresponding sequences of farnesyl diphosphate synthase from human, rat, Arabidopsis thaliana and Saccharomyces cerevisiae
