KEGG   ENZYME: 5.5.1.12Help
Entry
EC 5.5.1.12                 Enzyme                                 

Name
copalyl diphosphate synthase;
(+)-copalyl-diphosphate lyase (decyclizing)
Class
Isomerases;
Intramolecular lyases;
Intramolecular lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
(+)-copalyl-diphosphate lyase (ring-opening)
Reaction(IUBMB)
geranylgeranyl diphosphate = (+)-copalyl diphosphate [RN:R06298]
Reaction(KEGG)
Substrate
geranylgeranyl diphosphate [CPD:C00353]
Product
(+)-copalyl diphosphate [CPD:C11901]
Comment
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 catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.131, miltiradiene synthase, while in the tree Abies grandis (grand fir) it is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.18, abietadiene synthase.
History
EC 5.5.1.12 created 2002, modified 2012
Pathway
Diterpenoid biosynthesis
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K12927  
abietadiene/neoabietadiene/copalyl diphosphate synthase
K14041  
levopimaradiene/copalyl diphosphate synthase
K14042  
isopimara-7,15-diene synthase /copalyl diphosphate synthase
K18113  
miltiradiene synthase / copalyl diphosphate synthase
K19571  
levopimaradiene/neoabietadiene/copalyl diphosphate synthase
Genes
SMO: 
Taxonomy
Reference
1  [PMID:11552804]
  Authors
Peters RJ, Ravn MM, Coates RM, Croteau RB.
  Title
Bifunctional abietadiene synthase: free diffusive transfer of the (+)-copalyl diphosphate intermediate between two distinct active sites.
  Journal
J. Am. Chem. Soc. 123 (2001) 8974-8.
  Sequence
Reference
2  [PMID:22027823]
  Authors
Sugai Y, Ueno Y, Hayashi K, Oogami S, Toyomasu T, Matsumoto S, Natsume M, Nozaki H, Kawaide H
  Title
Enzymatic (13)C labeling and multidimensional NMR analysis of miltiradiene synthesized by bifunctional diterpene cyclase in Selaginella moellendorffii.
  Journal
J. Biol. Chem. 286 (2011) 42840-7.
  Sequence
Reference
3  [PMID:11805316]
  Authors
Peters RJ, Croteau RB.
  Title
Abietadiene synthase catalysis: mutational analysis of a prenyl diphosphate ionization-initiated cyclization and rearrangement.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 580-4.
  Sequence
Reference
4  [PMID:12059223]
  Authors
Ravn MM, Peters RJ, Coates RM, Croteau R.
  Title
Mechanism of abietadiene synthase catalysis: stereochemistry and stabilization of the cryptic pimarenyl carbocation intermediates.
  Journal
J. Am. Chem. Soc. 124 (2002) 6998-7006.
Reference
5  [PMID:11827528]
  Authors
Peters RJ, Croteau RB.
  Title
Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate.
  Journal
Biochemistry. 41 (2002) 1836-42.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
157972-08-2

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