CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 1 | Mainly Alpha | 
|   | 1.10 | Orthogonal Bundle | 
|   | 1.10.600 | Farnesyl Diphosphate Synthase | 
|   | 1.10.600.10 | Farnesyl Diphosphate Synthase | 
Domain Context
CATH Clusters
| Superfamily | Farnesyl Diphosphate Synthase | 
| Functional Family | Isoprene synthase, chloroplastic | 
Enzyme Information
| 4.2.3.116 | (+)-camphene synthase. based on mapping to UniProt O81192 Geranyl diphosphate = (+)-camphene + diphosphate. -!- Cyclase I of Salvia officinalis (sage) gives about equal parts (+)- camphene and (+)-alpha-pinene. -!- (3R)-linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. -!- See also EC 4.2.3.121. | 
| 4.2.3.121 | (+)-alpha-pinene synthase. based on mapping to UniProt O81192 Geranyl diphosphate = (+)-alpha-pinene + diphosphate. -!- Cyclase I of Salvia officinalis (sage) gives about equal parts (+)- alpha-pinene and (+)-camphene, whereas cyclase III gives about equal parts of (+)-alpha-pinene and (+)-beta-pinene. -!- (3R)-linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. -!- The 4-pro-R hydrogen of geranyl diphosphate is lost. -!- With synthase II of Pinus taeda (loblolly pine) (+)-beta-pinene was the only product. -!- See also EC 4.2.3.122 and EC 4.2.3.116. | 
| 5.5.1.8 | (+)-bornyl diphosphate synthase. based on mapping to UniProt O81192 Geranyl diphosphate = (+)-bornyl diphosphate. -!- The enzyme from Salvia officinalis (sage) can also use (3R)-linalyl diphosphate or more slowly neryl diphosphate in vitro. -!- The reaction proceeds via isomeration of geranyl diphosphate to (3R)- linalyl diphosphate. -!- The oxygen and phosphorus originally linked to C-1 of geranyl diphosphate end up linked to C-2 of (+)-bornyl diphosphate. -!- cf. EC 5.5.1.22. | 
UniProtKB Entries (1)
| O81192 | BPPS_SALOF Salvia officinalis (+)-bornyl diphosphate synthase, chloroplastic | 
PDB Structure
| PDB | 1N24 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | Escherichia | 
| Primary Citation | Bornyl diphosphate synthase:  Structure and strategy for carbocation manipulation by a terpenoid cyclase Proc.Natl.Acad.Sci.USA | 
