CATH Classification

Domain Context

CATH Clusters

Superfamily 1.50.10.160
Functional Family

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.
Zhou, K., Gao, Y., Hoy, J.A., Mann, F.M., Honzatko, R.B., Peters, R.J.
J.Biol.Chem.