KEGG   ENZYME: 5.5.1.8Help
Entry
EC 5.5.1.8                  Enzyme                                 

Name
(+)-bornyl diphosphate synthase;
bornyl pyrophosphate synthase;
bornyl pyrophosphate synthetase;
(+)-bornylpyrophosphate cyclase;
geranyl-diphosphate cyclase (ambiguous)
Class
Isomerases;
Intramolecular lyases;
Intramolecular lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
(+)-bornyl-diphosphate lyase (decyclizing)
Reaction(IUBMB)
geranyl diphosphate = (+)-bornyl diphosphate [RN:R02007]
Reaction(KEGG)
Substrate
geranyl diphosphate [CPD:C00341]
Product
(+)-bornyl diphosphate [CPD:C03190]
Comment
Requires Mg2+. The enzyme from Salvia officinalis (sage) can also use (3R)-linalyl diphosphate or more slowly neryl diphosphate in vitro [3]. The reaction proceeds via isomeration of geranyl diphosphate to (3R)-linalyl diphosphate. The oxygen and phosphorus originally linked to C-1 of geranyl diphosphate end up linked to C-2 of (+)-bornyl diphosphate [3]. cf. EC 5.5.1.22 [(-)-bornyl diphosphate synthase].
History
EC 5.5.1.8 created 1984, modified 2012
Pathway
Monoterpenoid biosynthesis
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K15098  
bornyl diphosphate synthase
Reference
1  [PMID:42356]
  Authors
Croteau R, Karp F.
  Title
Biosynthesis of monoterpenes: preliminary characterization of bornyl pyrophosphate synthetase from sage (Salvia officinalis) and demonstration that Geranyl pyrophosphate is the preferred substrate for cyclization.
  Journal
Arch. Biochem. Biophys. 198 (1979) 512-22.
  Organism
Salvia officinalis
Reference
2  [PMID:2178556]
  Authors
Croteau R, Gershenzon J, Wheeler CJ, Satterwhite DM
  Title
Biosynthesis of monoterpenes: stereochemistry of the coupled isomerization and cyclization of geranyl pyrophosphate to camphane and isocamphane monoterpenes.
  Journal
Arch. Biochem. Biophys. 277 (1990) 374-81.
Reference
3  [PMID:3759972]
  Authors
Croteau R, Satterwhite DM, Cane DE, Chang CC
  Title
Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of  (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-bornyl pyrophosphate.
  Journal
J. Biol. Chem. 261 (1986) 13438-45.
Reference
4  [PMID:3997807]
  Authors
Croteau R, Felton NM, Wheeler CJ
  Title
Stereochemistry at C-1 of geranyl pyrophosphate and neryl pyrophosphate in the cyclization to (+)- and (-)-bornyl pyrophosphate.
  Journal
J. Biol. Chem. 260 (1985) 5956-62.
Reference
5  [PMID:4084562]
  Authors
Croteau RB, Shaskus JJ, Renstrom B, Felton NM, Cane DE, Saito A, Chang C
  Title
Mechanism of the pyrophosphate migration in the enzymatic cyclization of geranyl  and linalyl pyrophosphates to (+)- and (-)-bornyl pyrophosphates.
  Journal
Biochemistry. 24 (1985) 7077-85.
Reference
6  [PMID:7872777]
  Authors
McGeady P, Croteau R
  Title
Isolation and characterization of an active-site peptide from a monoterpene cyclase labeled with a mechanism-based inhibitor.
  Journal
Arch. Biochem. Biophys. 317 (1995) 149-55.
Reference
7  [PMID:9614092]
  Authors
Wise ML, Savage TJ, Katahira E, Croteau R.
  Title
Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase.
  Journal
J. Biol. Chem. 273 (1998) 14891-9.
  Organism
Salvia officinalis
  Sequence
[up:O81192]
Reference
8  [PMID:12432096]
  Authors
Whittington DA, Wise ML, Urbansky M, Coates RM, Croteau RB, Christianson DW.
  Title
Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 15375-80.
  Organism
Salvia officinalis
  Sequence
[up:O81192]
Reference
9  [PMID:12941302]
  Authors
Peters RJ, Croteau RB
  Title
Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases.
  Journal
Arch. Biochem. Biophys. 417 (2003) 203-11.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
72668-91-8

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