(−)-beta-pinene synthase

{{Short description|Enzyme}}

{{Infobox enzyme

| Name = (−)-β-pinene synthase

| EC_number = 4.2.3.120

| CAS_number =

| GO_code =

| image =

| width =

| caption =

}}

(−)-β-Pinene synthase (EC 4.2.3.120, β-geraniolene synthase, (−)-(1S,5S)-pinene synthase, geranyldiphosphate diphosphate lyase (pinene forming)) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (−)-β-pinene-forming].{{cite journal | vauthors = Croteau RB, Wheeler CJ, Cane DE, Ebert R, Ha HJ | title = Isotopically sensitive branching in the formation of cyclic monoterpenes: proof that (–)-α-pinene and (–)-β-pinene are synthesized by the same monoterpene cyclase via deprotonation of a common intermediate | journal = Biochemistry | volume = 26 | issue = 17 | pages = 5383–9 | date = August 1987 | pmid = 3314988 | doi = 10.1021/bi00391a025 }}{{cite journal | vauthors = Croteau R, Satterwhite DM | title = Biosynthesis of monoterpenes. Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (–)-pinene cyclases from sage | journal = The Journal of Biological Chemistry | volume = 264 | issue = 26 | pages = 15309–15 | date = September 1989 | doi = 10.1016/S0021-9258(19)84827-5 | doi-access = free | pmid = 2768265 }}{{cite journal | vauthors = 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 = The Journal of Biological Chemistry | volume = 263 | issue = 21 | pages = 10063–71 | date = July 1988 | doi = 10.1016/S0021-9258(19)81477-1 | doi-access = free | pmid = 3392006 }}{{cite journal | vauthors = Pyun HJ, Wagschal KC, Jung DI, Coates RM, Croteau R | title = Stereochemistry of the proton elimination in the formation of (+)- and (–)-α-pinene by monoterpene cyclases from sage (Salvia officinalis) | journal = Archives of Biochemistry and Biophysics | volume = 308 | issue = 2 | pages = 488–96 | date = February 1994 | pmid = 8109979 | doi = 10.1006/abbi.1994.1069 }}{{cite journal | vauthors = Lu S, Xu R, Jia JW, Pang J, Matsuda SP, Chen XY | title = Cloning and functional characterization of a β-pinene synthase from Artemisia annua that shows a circadian pattern of expression | journal = Plant Physiology | volume = 130 | issue = 1 | pages = 477–86 | date = September 2002 | pmid = 12226526 | pmc = 166579 | doi = 10.1104/pp.006544 }}{{cite journal | vauthors = Gijzen M, Lewinsohn E, Croteau R | title = Characterization of the constitutive and wound-inducible monoterpene cyclases of grand fir (Abies grandis) | journal = Archives of Biochemistry and Biophysics | volume = 289 | issue = 2 | pages = 267–73 | date = September 1991 | pmid = 1898071 | doi = 10.1016/0003-9861(91)90471-T }}{{cite journal | vauthors = Lewinsohn E, Gijzen M, Croteau R | title = Wound-inducible pinene cyclase from grand fir: purification, characterization, and renaturation after SDS-PAGE | journal = Archives of Biochemistry and Biophysics | volume = 293 | issue = 1 | pages = 167–73 | date = February 1992 | pmid = 1731633 | doi = 10.1016/0003-9861(92)90380-f }}{{cite journal | vauthors = Bohlmann J, Steele CL, Croteau R | title = Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (–)-(4S)-limonene synthase, and (–)-(1S,5S)-pinene synthase | journal = The Journal of Biological Chemistry | volume = 272 | issue = 35 | pages = 21784–92 | date = August 1997 | pmid = 9268308 | doi = 10.1074/jbc.272.35.21784 | doi-access = free }}{{cite journal | vauthors = Hyatt DC, Croteau R | title = Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis | journal = Archives of Biochemistry and Biophysics | volume = 439 | issue = 2 | pages = 222–33 | date = July 2005 | pmid = 15978541 | doi = 10.1016/j.abb.2005.05.017 }}{{cite journal | vauthors = Savage TJ, Ichii H, Hume SD, Little DB, Croteau R | title = Monoterpene synthases from gymnosperms and angiosperms: stereospecificity and inactivation by cysteinyl- and arginyl-directed modifying reagents | journal = Archives of Biochemistry and Biophysics | volume = 320 | issue = 2 | pages = 257–65 | date = July 1995 | pmid = 7625832 | doi = 10.1016/0003-9861(95)90008-x }}{{cite journal | vauthors = Phillips MA, Savage TJ, Croteau R | title = Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers | journal = Archives of Biochemistry and Biophysics | volume = 372 | issue = 1 | pages = 197–204 | date = December 1999 | pmid = 10562434 | doi = 10.1006/abbi.1999.1467 }}{{cite journal | vauthors = McKay SA, Hunter WL, Godard KA, Wang SX, Martin DM, Bohlmann J, Plant AL | title = Insect attack and wounding induce traumatic resin duct development and gene expression of (-)-pinene synthase in Sitka spruce | journal = Plant Physiology | volume = 133 | issue = 1 | pages = 368–78 | date = September 2003 | pmid = 12970502 | pmc = 196613 | doi = 10.1104/pp.103.022723 }} This enzyme catalyses the following chemical reaction

: geranyl diphosphate $\backslash rightleftharpoons$ (−)-β-pinene + diphosphate

Cyclase II of Salvia officinalis (sage) produces about equal parts (−)-α-pinene, (−)-β-pinene and (−)-camphene.