(−)-beta-pinene synthase

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(−)-β-pinene synthase
Identifiers
EC no. 4.2.3.120
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(−)-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]. [1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] This enzyme catalyses the following chemical reaction

geranyl diphosphate (−)-β-pinene + diphosphate

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

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The enzyme myrcene synthase catalyzes the chemical reaction

In enzymology, a pinene synthase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Terpene synthase N terminal domain</span> Protein domain

In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes, which are part of primary metabolism, such as sterols and carotene, and also part of the secondary metabolism. This entry will focus on the N terminal domain of the TPS protein.

<span class="mw-page-title-main">Terpene synthase C terminal domain</span> Protein domain

In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes, which are part of primary metabolism, such as sterols and carotene, and also part of the secondary metabolism. This entry will focus on the C terminal domain of the TPS protein.

β-Phellandrene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

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(+)-δ-Selinene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ( -δ-selinene-forming). This enzyme catalyses the following chemical reaction

(+)-Car-3-ene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-car-3-ene-forming]. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">1,8-cineole synthase</span>

1,8-Cineole synthase (EC 4.2.3.108, 1,8-cineole cyclase, geranyl pyrophoshate:1,8-cineole cyclase, 1,8-cineole synthetase) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase (cyclizing, 1,8-cineole-forming). This enzyme catalyses the following chemical reaction

(−)-Sabinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (−)-sabinene-forming]. This enzyme catalyses the following chemical reaction

(+)-Sabinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-sabinene-forming]. This enzyme catalyses the following chemical reaction

Terpinolene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

γ-Terpinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

(+)-camphene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-camphene-forming]. This enzyme catalyses the following chemical reaction

(−)-camphene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (−)-camphene-forming]. This enzyme catalyses the following chemical reaction

(−)-α-Pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (−)-α-pinene-forming]. This enzyme catalyses the following chemical reaction

(+)-α-pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-α-pinene-forming]. This enzyme catalyses the following chemical reaction

(+)-β-Pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [(+)-β-pinene-forming]. This enzyme catalyses the following chemical reaction

References

  1. Croteau RB, Wheeler CJ, Cane DE, Ebert R, Ha HJ (August 1987). "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". Biochemistry. 26 (17): 5383–9. doi:10.1021/bi00391a025. PMID   3314988.
  2. Croteau R, Satterwhite DM (September 1989). "Biosynthesis of monoterpenes. Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (–)-pinene cyclases from sage". The Journal of Biological Chemistry. 264 (26): 15309–15. doi: 10.1016/S0021-9258(19)84827-5 . PMID   2768265.
  3. 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. doi: 10.1016/S0021-9258(19)81477-1 . PMID   3392006.
  4. 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.
  5. Lu S, Xu R, Jia JW, Pang J, Matsuda SP, Chen XY (September 2002). "Cloning and functional characterization of a β-pinene synthase from Artemisia annua that shows a circadian pattern of expression". Plant Physiology. 130 (1): 477–86. doi:10.1104/pp.006544. PMC   166579 . PMID   12226526.
  6. Gijzen M, Lewinsohn E, Croteau R (September 1991). "Characterization of the constitutive and wound-inducible monoterpene cyclases of grand fir (Abies grandis)". Archives of Biochemistry and Biophysics. 289 (2): 267–73. doi:10.1016/0003-9861(91)90471-T. PMID   1898071.
  7. Lewinsohn E, Gijzen M, Croteau R (February 1992). "Wound-inducible pinene cyclase from grand fir: purification, characterization, and renaturation after SDS-PAGE". Archives of Biochemistry and Biophysics. 293 (1): 167–73. doi:10.1016/0003-9861(92)90380-f. PMID   1731633.
  8. Bohlmann J, Steele CL, Croteau R (August 1997). "Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (–)-(4S)-limonene synthase, and (–)-(1S,5S)-pinene synthase". The Journal of Biological Chemistry. 272 (35): 21784–92. doi: 10.1074/jbc.272.35.21784 . PMID   9268308.
  9. Hyatt DC, Croteau R (July 2005). "Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis". Archives of Biochemistry and Biophysics. 439 (2): 222–33. doi:10.1016/j.abb.2005.05.017. PMID   15978541.
  10. Savage TJ, Ichii H, Hume SD, Little DB, Croteau R (July 1995). "Monoterpene synthases from gymnosperms and angiosperms: stereospecificity and inactivation by cysteinyl- and arginyl-directed modifying reagents". Archives of Biochemistry and Biophysics. 320 (2): 257–65. doi:10.1016/0003-9861(95)90008-x. PMID   7625832.
  11. 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.
  12. McKay SA, Hunter WL, Godard KA, Wang SX, Martin DM, Bohlmann J, Plant AL (September 2003). "Insect attack and wounding induce traumatic resin duct development and gene expression of (-)-pinene synthase in Sitka spruce". Plant Physiology. 133 (1): 368–78. doi:10.1104/pp.103.022723. PMC   196613 . PMID   12970502.