KEGG   ENZYME: 5.5.1.8Help
Entry
EC 5.5.1.8                  Enzyme                                 

Name
(+)-bornyl diphosphate synthase;
bornyl pyrophosphate synthase (ambiguous);
bornyl pyrophosphate synthetase (ambiguous);
(+)-bornylpyrophosphate cyclase;
geranyl-diphosphate cyclase (ambiguous);
(+)-bornyl-diphosphate lyase (decyclizing)
Class
Isomerases;
Intramolecular lyases;
Intramolecular lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
(+)-bornyl-diphosphate lyase (ring-opening)
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
ec00902  Monoterpenoid biosynthesis
ec01100  Metabolic pathways
ec01110  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 198:512-22 (1979)
DOI:10.1016/0003-9861(79)90526-5
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 277:374-81 (1990)
DOI:10.1016/0003-9861(90)90593-N
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 261:13438-45 (1986)
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 260:5956-62 (1985)
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 24:7077-85 (1985)
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 317:149-55 (1995)
DOI:10.1006/abbi.1995.1147
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 273:14891-9 (1998)
DOI:10.1074/jbc.273.24.14891
  Sequence
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 99:15375-80 (2002)
DOI:10.1073/pnas.232591099
  Sequence
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 417:203-11 (2003)
DOI:10.1016/S0003-9861(03)00347-3
Other DBs
ExplorEnz - The Enzyme Database: 5.5.1.8
IUBMB Enzyme Nomenclature: 5.5.1.8
ExPASy - ENZYME nomenclature database: 5.5.1.8
BRENDA, the Enzyme Database: 5.5.1.8
CAS: 72668-91-8

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