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CATH Classification

Domain Context

CATH Clusters

Superfamily Farnesyl Diphosphate Synthase
Functional Family Geranylgeranyl pyrophosphate synthase

Enzyme Information

2.5.1.10
(2E,6E)-farnesyl diphosphate synthase.
based on mapping to UniProt O95749
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)- farnesyl diphosphate.
-!- Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate. -!- The enzyme will not accept larger prenyl diphosphates as efficient donors.
2.5.1.29
Geranylgeranyl diphosphate synthase.
based on mapping to UniProt O95749
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate.
-!- Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors.
2.5.1.1
Dimethylallyltranstransferase.
based on mapping to UniProt O95749
Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.
-!- Will not accept larger prenyl diphosphates as efficient donors.
2.5.1.-
Transferring alkyl or aryl groups, other than methyl groups.
based on mapping to UniProt O95749

UniProtKB Entries (1)

O95749
GGPPS_HUMAN
Homo sapiens
Geranylgeranyl pyrophosphate synthase

PDB Structure

PDB 2Q80
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding
Kavanagh, K.L., Dunford, J.E., Bunkoczi, G., Russell, R.G., Oppermann, U.
J.Biol.Chem.
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