KEGG   ENZYME: 4.2.3.32Help
Entry
EC 4.2.3.32                 Enzyme                                 

Name
levopimaradiene synthase;
PtTPS-LAS;
LPS;
copalyl-diphosphate diphosphate-lyase [abieta-8(14),12-diene-forming]
Class
Lyases;
Carbon-oxygen lyases;
Acting on phosphates
BRITE hierarchy
Sysname
(+)-copalyl-diphosphate diphosphate-lyase [abieta-8(14),12-diene-forming]
Reaction(IUBMB)
(+)-copalyl diphosphate = abieta-8(14),12-diene + diphosphate [RN:R06302]
Reaction(KEGG)
R06302;
(other) R06304
Show
Substrate
(+)-copalyl diphosphate [CPD:C11901]
Product
abieta-8(14),12-diene [CPD:C11879];
diphosphate [CPD:C00013]
Comment
In Ginkgo, the enzyme catalyses the initial cyclization step in the biosynthesis of ginkgolides, a structurally unique family of diterpenoids that are highly specific platelet-activating-factor receptor antagonists [1]. Levopimaradiene is widely distributed in higher plants. In some species the enzyme also forms abietadiene, palustradiene, and neoabietadiene [2].
History
EC 4.2.3.32 created 2008, modified 2012
Pathway
Diterpenoid biosynthesis
Biosynthesis of secondary metabolites
Orthology
K14041  
levopimaradiene/copalyl diphosphate synthase
K19571  
levopimaradiene/neoabietadiene/copalyl diphosphate synthase
Reference
1  [PMID:11488601]
  Authors
Schepmann HG, Pang J, Matsuda SP.
  Title
Cloning and characterization of Ginkgo biloba levopimaradiene synthase which catalyzes the first committed step in ginkgolide biosynthesis.
  Journal
Arch. Biochem. Biophys. 392 (2001) 263-9.
  Sequence
Reference
2  [PMID:16497345]
  Authors
Ro DK, Bohlmann J.
  Title
Diterpene resin acid biosynthesis in loblolly pine (Pinus taeda): functional characterization of abietadiene/levopimaradiene synthase (PtTPS-LAS) cDNA and subcellular targeting of PtTPS-LAS and abietadienol/abietadienal oxidase (PtAO, CYP720B1).
  Journal
Phytochemistry. 67 (2006) 1572-8.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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