KEGG   ENZYME: 4.2.3.36Help
Entry
EC 4.2.3.36                 Enzyme                                 

Name
terpentetriene synthase;
Cyc2
Class
Lyases;
Carbon-oxygen lyases;
Acting on phosphates
BRITE hierarchy
Sysname
terpentedienyl-diphosphate diphosphate-lyase (terpentetriene-forming)
Reaction(IUBMB)
terpentedienyl diphosphate = terpentetriene + diphosphate [RN:R09684]
Reaction(KEGG)
Substrate
terpentedienyl diphosphate [CPD:C19815]
Product
terpentetriene [CPD:C19814];
diphosphate [CPD:C00013]
Comment
Requires Mg2+ for maximal activity but can use Mn2+, Fe2+ or Co2+ to a lesser extent [2]. Following on from EC 5.5.1.15, terpentedienyl-diphosphate synthase, this enzyme completes the transformation of geranylgeranyl diphosphate (GGDP) into terpentetriene, which is a precursor of the diterpenoid antibiotic terpentecin. Farnesyl diphosphate can also act as a substrate.
History
EC 4.2.3.36 created 2008
Pathway
Biosynthesis of antibiotics
Orthology
K19834  
terpentetriene synthase
Reference
1  [PMID:11567009]
  Authors
Dairi T, Hamano Y, Kuzuyama T, Itoh N, Furihata K, Seto H.
  Title
Eubacterial diterpene cyclase genes essential for production of the isoprenoid antibiotic terpentecin.
  Journal
J. Bacteriol. 183 (2001) 6085-94.
  Sequence
Reference
2  [PMID:12138123]
  Authors
Hamano Y, Kuzuyama T, Itoh N, Furihata K, Seto H, Dairi T.
  Title
Functional analysis of eubacterial diterpene cyclases responsible for biosynthesis of a diterpene antibiotic, terpentecin.
  Journal
J. Biol. Chem. 277 (2002) 37098-104.
  Sequence
Reference
3  [PMID:12839434]
  Authors
Eguchi T, Dekishima Y, Hamano Y, Dairi T, Seto H, Kakinuma K.
  Title
A new approach for the investigation of isoprenoid biosynthesis featuring pathway switching, deuterium hyperlabeling, and 1H NMR spectroscopy. The reaction mechanism of a novel streptomyces diterpene cyclase.
  Journal
J. Org. Chem. 68 (2003) 5433-8.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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