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Information on EC 2.5.1.10 - (2E,6E)-farnesyl diphosphate synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P08524

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IUBMB Comments
Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate. The enzyme will not accept larger prenyl diphosphates as efficient donors.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P08524
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
farnesyl diphosphate synthase, farnesyl pyrophosphate synthase, fpp synthase, erg20, farnesyl pyrophosphate synthetase, hfpps, farnesyl-diphosphate synthase, fppase, fpps1, fpps3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
farnesyl diphosphate synthase
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farnesyl pyrophosphate synthetase
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farnesyl-diphosphate synthase
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farnesylpyrophosphate synthetase
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geranyl transferase I
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geranyltranstransferase
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prenyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkenyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate:isopentenyl-diphosphate geranyltranstransferase
Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate. The enzyme will not accept larger prenyl diphosphates as efficient donors.
CAS REGISTRY NUMBER
COMMENTARY hide
37277-79-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + isopentenyl diphosphate
diphosphate + geranyl diphosphate
show the reaction diagram
geranyl diphosphate + isopentenyl diphosphate
diphosphate + (2E,6E)-farnesyl diphosphate
show the reaction diagram
geranyl diphosphate + isopentenyl diphosphate
diphosphate + farnesyl diphosphate
show the reaction diagram
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?
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
dimethylallyl diphosphate + isopentenyl diphosphate
diphosphate + geranyl diphosphate
show the reaction diagram
geranyl diphosphate + isopentenyl diphosphate
diphosphate + (2E,6E)-farnesyl diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
contains 3 Mg2+ ions
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
farnesyl diphosphate synthase is a key enzyme responsible for the supply of isoprenoid precursors for several essential metabolites, including sterols, dolichols and ubiquinone
physiological function
key enzyme responsible for the supply of isoprenoid precursors for several essential metabolites, including sterols, dolichols and ubiquinone
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, affinity chromatography
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bartlett, D.L.; King, C.H.R.; Poulter, C.D.
Purification of farnesylpyrophosphate synthetase by affinity chromatography
Methods Enzymol.
110
171-184
1985
Saccharomyces cerevisiae, Gallus gallus
Manually annotated by BRENDA team
Fischer, M.J.; Meyer, S.; Claudel, P.; Bergdoll, M.; Karst, F.
Identification of a lysine residue important for the catalytic activity of yeast farnesyl diphosphate synthase
Protein J.
30
334-339
2011
Saccharomyces cerevisiae (P08524), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Rubat, S.; Varas, I.; Sepulveda, R.; Almonacid, D.; Gonzalez-Nilo, F.; Agosin, E.
Increasing the intracellular isoprenoid pool in Saccharomyces cerevisiae by structural fine-tuning of a bifunctional farnesyl diphosphate synthase
FEMS Yeast Res.
17
fox032
2017
Saccharomyces cerevisiae (P08524), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741 (P08524)
Manually annotated by BRENDA team