(+)-α-pinene synthase (EC 4.2.3.121, (+)-α-pinene cyclase, cyclase I) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-α-pinene-forming].[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
| (+)-α-pinene synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.3.121 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-α-pinene and (+)-camphene.
References
edit- ^ Gambliel H, Croteau R (January 1984). "Pinene cyclases I and II. Two enzymes from sage (Salvia officinalis) which catalyze stereospecific cyclizations of geranyl pyrophosphate to monoterpene olefins of opposite configuration". The Journal of Biological Chemistry. 259 (2): 740–8. PMID 6693393.
- ^ Croteau R, Satterwhite DM, Cane DE, Chang CC (July 1988). "Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (–)-linalyl pyrophosphate to (+)- and (–)-pinene and (+)- and (–)-camphene". The Journal of Biological Chemistry. 263 (21): 10063–71. PMID 3392006.
- ^ Wagschal KC, Pyun HJ, Coates RM, Croteau R (February 1994). "Monoterpene biosynthesis: isotope effects associated with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis)". Archives of Biochemistry and Biophysics. 308 (2): 477–87. doi:10.1006/abbi.1994.1068. PMID 8109978.
- ^ Pyun HJ, Wagschal KC, Jung DI, Coates RM, Croteau R (February 1994). "Stereochemistry of the proton elimination in the formation of (+)- and (–)-α-pinene by monoterpene cyclases from sage (Salvia officinalis)". Archives of Biochemistry and Biophysics. 308 (2): 488–96. doi:10.1006/abbi.1994.1069. PMID 8109979.
- ^ Phillips MA, Savage TJ, Croteau R (December 1999). "Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers". Archives of Biochemistry and Biophysics. 372 (1): 197–204. doi:10.1006/abbi.1999.1467. PMID 10562434.
- ^ Phillips MA, Wildung MR, Williams DC, Hyatt DC, Croteau R (March 2003). "cDNA isolation, functional expression, and characterization of (+)-α-pinene synthase and (-)-α-pinene synthase from loblolly pine (Pinus taeda): stereocontrol in pinene biosynthesis". Archives of Biochemistry and Biophysics. 411 (2): 267–76. doi:10.1016/s0003-9861(02)00746-4. PMID 12623076.
External links
edit- (+)-alpha-pinene+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
