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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
ec00904  Diterpenoid biosynthesis
ec01100  Metabolic pathways
ec01110  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
K20514  phyllocladan-16alpha-ol/copalyl diphosphate synthase
Genes
SMO: SELMODRAFT_450918
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 123:8974-8 (2001)
DOI:10.1021/ja010670k
  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 286:42840-7 (2011)
DOI:10.1074/jbc.M111.302703
  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 99:580-4 (2002)
DOI:10.1073/pnas.022627099
  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 124:6998-7006 (2002)
DOI:10.1021/ja017734b
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 41:1836-42 (2002)
DOI:10.1021/bi011879d
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 5.5.1.12
IUBMB Enzyme Nomenclature: 5.5.1.12
ExPASy - ENZYME nomenclature database: 5.5.1.12
BRENDA, the Enzyme Database: 5.5.1.12
CAS: 157972-08-2

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