CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.50 | Alpha/alpha barrel | |
1.50.10 | Glycosyltransferase | |
1.50.10.130 | Terpene synthase, N-terminal domain |
Domain Context
CATH Clusters
Superfamily | Terpene synthase, N-terminal domain |
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.
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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.
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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.
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UniProtKB Entries (1)
O81192 |
BPPS_SALOF
Salvia officinalis
(+)-bornyl diphosphate synthase, chloroplastic
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PDB Structure
PDB | 1N20 |
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
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