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Information on EC 2.5.1.10 - (2E,6E)-farnesyl diphosphate synthase

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EC Tree
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:
UNIPROT: Q8WS25
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Word Map
The enzyme appears in 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 pyrophosphate 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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8WS25_TRYCR
316
0
35735
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystallization data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with substrate isopentenyl diphosphate and five nitrogen-containing bisphosphonate inhibitors. The C1-hydroxyl and the nitrogen-containing groups of the inhibitors alter the binding of isopentenyl diphosphate and the conformation of residues Y94 and Q167. binding of the inhibitors changes the binding properties of the second site of the dimer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
farnesyl pyrophosphate synthase as a target for fragment-based lead discovery has revealed that it can be used for fragment library screening and hit validation using an unconventional referencing, suitable when reference compounds are not available
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, C.H.; Gabelli, S.B.; Oldfield, E.; Amzel, L.M.
Binding of nitrogen-containing bisphosphonates (N-BPs) to the Trypanosoma cruzi farnesyl diphosphate synthase homodimer
Proteins
78
888-899
2010
Trypanosoma cruzi (Q8WS25), Trypanosoma cruzi
Manually annotated by BRENDA team
Opassi, G.; Nordstroem, H.; Lundin, A.; Napolitano, V.; Magari, F.; Dzus, T.; Klebe, G.; Danielson, U.H.
Establishing Trypanosoma cruzi farnesyl pyrophosphate synthase as a viable target for biosensor driven fragment-based lead discovery
Protein Sci.
29
991-1003
2020
Trypanosoma cruzi (Q8WS25), Trypanosoma cruzi
Manually annotated by BRENDA team