Information on EC 2.5.1.81 - geranylfarnesyl diphosphate synthase

New: Word Map on EC 2.5.1.81
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Archaea

EC NUMBER
COMMENTARY hide
2.5.1.81
-
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
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
isoprenoid biosynthesis
-
-
ophiobolin F biosynthesis
-
-
stellatic acid biosynthesis
-
-
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
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
?
-
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
-
-
?
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
-
-
?
geranylgeranyl diphosphate + isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
maximal activity around 5.0 mM, no activity with other divalent cations such as Ca2+, Mn2+, and Zn2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48900
gel filtration
76000
-
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a glutathione S-transferase fusion protein
-
expression of wild-type and mutant enzymes in Escherichia coli
-
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
-
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