KEGG   ENZYME: 4.2.3.116Help
Entry
EC 4.2.3.116                Enzyme                                 

Name
(+)-camphene synthase
Class
Lyases;
Carbon-oxygen lyases;
Acting on phosphates
BRITE hierarchy
Sysname
geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-camphene-forming]
Reaction(IUBMB)
geranyl diphosphate = (+)-camphene + diphosphate [RN:R09971]
Reaction(KEGG)
Substrate
geranyl diphosphate [CPD:C00341]
Product
(+)-camphene [CPD:C06304];
diphosphate [CPD:C00013]
Comment
Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-camphene and (+)-alpha-pinene. (3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. Requires Mg2+ (preferred to Mn2+). See also EC 4.2.3.121 (+)-alpha-pinene synthase.
History
EC 4.2.3.116 created 2012
Reference
1  [PMID:6693393]
  Authors
Gambliel H, Croteau R
  Title
Pinene cyclases I and II. Two enzymes from sage (Salvia officinalis) which catalyze stereospecific cyclizations of geranyl pyrophosphate to monoterpene olefins of opposite configuration.
  Journal
J. Biol. Chem. 259 (1984) 740-8.
Reference
2  [PMID:3392006]
  Authors
Croteau R, Satterwhite DM, Cane DE, Chang CC
  Title
Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of  (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-pinene and (+)- and (-)-camphene.
  Journal
J. Biol. Chem. 263 (1988) 10063-71.
Reference
3  [PMID:8109978]
  Authors
Wagschal KC, Pyun HJ, Coates RM, Croteau R.
  Title
Monoterpene biosynthesis: isotope effects associated with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis).
  Journal
Arch. Biochem. Biophys. 308 (1994) 477-87.
Reference
4  [PMID:8109979]
  Authors
Pyun HJ, Wagschal KC, Jung DI, Coates RM, Croteau R
  Title
Stereochemistry of the proton elimination in the formation of (+)- and (-)-alpha-pinene by monoterpene cyclases from sage (Salvia officinalis).
  Journal
Arch. Biochem. Biophys. 308 (1994) 488-96.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
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BRENDA, the Enzyme Database: 

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