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 | Ent-copalyl diphosphate synthase, chloroplastic |
Enzyme Information
| 4.2.3.132 |
Neoabietadiene synthase.
based on mapping to UniProt Q38710
(+)-copalyl diphosphate = neoabietadiene + diphosphate.
-!- Isolated from Abies grandis (grand fir). -!- This class I enzyme forms about equal proportions of abietadiene, levopimaradiene and neoabietadiene; see also EC 4.2.3.18 and EC 4.2.3.32. -!- An X-ray study of this multifunctional enzyme showed that the class I activity is in the alpha domain, while EC 5.5.1.12 activity (a class II activity) is in the beta and gamma domains. -!- In Pinus taeda (loblolly pine) the major product is levopimaradiene, with less abietadiene and neoabietadiene.
|
| 5.5.1.12 |
Copalyl diphosphate synthase.
based on mapping to UniProt Q38710
Geranylgeranyl diphosphate = (+)-copalyl diphosphate.
-!- In some plants, such as Salvia miltiorrhiza, this enzyme is monofunctional. -!- In other plants this activity is often a part of a bifunctional enzyme. -!- For example, in Selaginella moellendorffii this activity is catalyzed by a bifunctional enzyme that also catalyzes EC 4.2.3.131, while in the tree Abies grandis (grand fir) it is catalyzed by a bifunctional enzyme that also catalyzes EC 4.2.3.18.
|
| 4.2.3.18 |
Abieta-7,13-diene synthase.
based on mapping to UniProt Q38710
(+)-copalyl diphosphate = abieta-7,13-diene + diphosphate.
-!- Part of a bifunctional enzyme involved in the biosynthesis of abietadiene. -!- See also EC 5.5.1.12.
|
UniProtKB Entries (1)
| Q38710 |
TPSDV_ABIGR
Abies grandis
Bifunctional abietadiene synthase, chloroplastic
|
PDB Structure
| PDB | 3S9V |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Insights into diterpene cyclization from structure of bifunctional abietadiene synthase from Abies grandis.
J.Biol.Chem.
|
