Information on EC 2.5.1.81 - geranylfarnesyl diphosphate synthase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
2.5.1.81
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RECOMMENDED NAME
GeneOntology No.
geranylfarnesyl diphosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ophiobolin F biosynthesis
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stellatic acid biosynthesis
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isoprenoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 1 isopentenyl unit)
The enzyme from Methanosarcina mazei is involved in biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis. It prefers geranylgeranyl diphosphate and farnesyl diphosphate as allylic substrate [1]. The enzyme from Aeropyrum pernix prefers farnesyl diphosphate as allylic substrate. The enzyme is involved in the biosynthesis of C25-C25 membrane lipids [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
gene Lc-GFDPS
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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phylogenetic analysis suggest that GFDPS probably evolved from plant geranylgeranyl diphosphate synthase under the influence of positive selection. Lc-GFDPS clusters in subcluster Ia, which is dominated by GGDPS sequences
malfunction
metabolism
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biosynthesis of the C25 precursor geranylfarnesyl diphosphate to leucosceptroid sesterterpenoids is catalyzed by enzyme GFDPS that uses substrates geranylgeranyl diphosphate and Iisopentenyl diphosphate derived from the plastidial MEP pathway, overview
physiological function
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the geranylfarnesyl diphosphate synthase provides the precursor for sesterterpenoid (C25) formation in the glandular trichomes of the mint species Leucosceptrum canum, the C25 terpenoids might play a defensive role
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + 2 isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + 2 diphosphate
show the reaction diagram
dimethylallyl diphosphate + 4 isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + 4 diphosphate
show the reaction diagram
farnesyl diphosphate + 2 isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + 2 diphosphate
show the reaction diagram
geranyl diphosphate + 3 isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + 3 diphosphate
show the reaction diagram
geranylgeranyl diphosphate + isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + 2 isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + 2 diphosphate
show the reaction diagram
Q9UWR6
Aeropyrum pernix does not possess geranylgeranyl diphosphate synthase and has only C25-C25 ether lipids, but no C20-containing ether lipids. Aeropyrum pernix farnesylgeranyl diphosphate synthase is important in the biosynthesis of the hydrocarbon moiety of membrane lipids
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-
?
farnesyl diphosphate + 2 isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + 2 diphosphate
show the reaction diagram
Q8PYS1
biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis
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?
geranylgeranyl diphosphate + isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no activation by Mg2+ and Mn2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tween 20
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highly activating
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00165 - 0.014
geranylgeranyl diphosphate
0.00304 - 0.011
isopentenyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000517
geranylgeranyl diphosphate
Leucosceptrum canum
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pH 7.5, 30°C
0.0000082
isopentenyl diphosphate
Leucosceptrum canum
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pH 7.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
geranylgeranyl diphosphate
Leucosceptrum canum
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pH 7.5, 30°C
231
0.0028
isopentenyl diphosphate
Leucosceptrum canum
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pH 7.5, 30°C
113
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
assay at; assay at; assay at; assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
high expression level
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
x * 33000, SDS-PAGE, calculated from sequence
33836
2 * 33836, calculated
48900
gel filtration
76000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 33000, SDS-PAGE, calculated from sequence
dimer
2 * 33836, calculated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
model structure of mutant I112A, calculated using the model of wild-type GFPS as a template. In wild-type enzyme, the I112 on each subunit is located next to the I112 on the other at the dimer interface, to separate the two reaction cavities. In the mutant enzyme, the substitution of I112 by alanine results in the formation of a large tunnel between dimer subunits, enabling prenyl diphosphates to elongate through the newly-created path from one cavity to the other, thus yielding extremely lengthened prenyl diphosphates
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged AtIDS1 from Escherichia coli strain BL21 by glutathione affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a glutathione S-transferase fusion protein
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expression of wild-type and mutant enzymes in Escherichia coli
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gene AtIDS10, recombinant overexpression of GST-tagged enzyme in Escherichia coli strain BL21, transient expression of N-terminally GFP-tagged enzyme in Nicotiana benthamiana; gene AtIDS1, recombinant overexpression of GST-tagged enzyme in Escherichia coli strain BL21, and recombinant enzyme expression in the loss-of-function AtIDS11 mutant ggpps11-4, which has an embryolethal phenotype due to the lack of GGDP. AtIDS1, a predominantly GFDP-producing enzyme that nonetheless forms a sizable amount of GGDP, complements the embryo-lethal phenotype of ggpps11-4. Transient expression of N-terminally GFP-tagged enzyme in Nicotiana benthamiana; gene AtIDS6, recombinant overexpression of GST-tagged enzyme in Escherichia coli strain BL21, transient expression of N-terminally GFP-tagged enzyme in Nicotiana benthamiana; gene AtIDS7, recombinant overexpression of GST-tagged enzyme in Escherichia coli strain BL21, transient expression of N-terminally GFP-tagged enzyme in Nicotiana benthamiana; gene AtIDS9, recombinant overexpression of GST-tagged enzyme in Escherichia coli strain BL21 and of N-terminally His6-tagged enzyme in Arabidopsis thaliana ecotype Col-0 under control of CaMV 35S promoter via Agrobacterium tumefaciens strain GV3101 transfection method, and recombinant enzyme expression in the loss-of-function AtIDS11 mutant ggpps11-4, which has an embryolethal phenotype due to the lack of GGDP. Transient expression of N-terminally GFP-tagged enzyme in Nicotiana benthamiana
gene Lc-GFDPS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional recombinant expression in Escherichia coli, and in Arabidopsis thaliana driven by a double CaMV 35S promoter
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
application of salicilic acid and methyl jasmonate induce GFDPS transcript and sesterterpenoid accumulation
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D109A
mutation leads to the production of longer prenyl diphosphates from C30 to C35, but at small rates
I112A
chain length of the products of mutant I112A reaches up to C70 or longer, which is three times as long as that of the wild type. A large fraction of the longer products is C45-50, which is nearly twice as long as wild-type
II116A
mutation leads to the production of longer prenyl diphosphates from C30 to C35, but at small rates
M137A
slight increase in chain length of products
M72A
slight increase in chain length of products
additional information
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directed evolution is used to create mutant FGPP synthases that confirm the importance of amino acids upstream of the FARM of prenyl diphosphate synthases and demonstrate the significance of mutations upstream of an additional conserved region (141GQ142). Product chain-length distribution can be also controlled by a structural change provoked by a cooperative interaction of amino acids