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Information on EC 2.5.1.81 - geranylfarnesyl diphosphate synthase and Organism(s) Methanosarcina mazei and UniProt Accession Q8PYS1

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IUBMB Comments
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 . The enzyme from Aeropyrum pernix prefers farnesyl diphosphate as allylic substrate. The enzyme is involved in the biosynthesis of C25-C25 membrane lipids .
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Methanosarcina mazei
UNIPROT: Q8PYS1
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The taxonomic range for the selected organisms is: Methanosarcina mazei
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Synonyms
geranylfarnesyl diphosphate synthase, fgpp synthase, gfdps, c25 farnesylgeranyl diphosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -, -
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
slight activity
-
-
?
geranylgeranyl diphosphate + isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
farnesyl diphosphate + 2 isopentenyl diphosphate
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + 2 diphosphate
show the reaction diagram
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
biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis
-
-
?
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
x * 33000, SDS-PAGE, calculated from sequence
33836
2 * 33836, calculated
48900
gel filtration
SUBUNIT
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
PROTEIN VARIANTS
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ogawa, T.; Yoshimura, T.; Hemmi, H.
Geranylfarnesyl diphosphate synthase from Methanosarcina mazei: Different role, different evolution
Biochem. Biophys. Res. Commun.
393
16-20
2010
Methanosarcina mazei (Q8PYS1), Methanosarcina mazei
Manually annotated by BRENDA team
Ogawa, T.; Yoshimura, T.; Hemmi, H.
Connected cavity structure enables prenyl elongation across the dimer interface in mutated geranylfarnesyl diphosphate synthase from Methanosarcina mazei
Biochem. Biophys. Res. Commun.
409
333-337
2011
Methanosarcina mazei (Q8PYS1), Methanosarcina mazei
Manually annotated by BRENDA team