Biology:(-)-beta-pinene synthase

From HandWiki
Short description: Enzyme
(–)-β-pinene synthase
Identifiers
EC number4.2.3.120
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

(–)-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 [math]\displaystyle{ \rightleftharpoons }[/math] (–)-β-pinene + diphosphate

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

References

  1. "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. August 1987. doi:10.1021/bi00391a025. PMID 3314988. 
  2. "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. September 1989. PMID 2768265. 
  3. "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. July 1988. PMID 3392006. 
  4. "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. February 1994. doi:10.1006/abbi.1994.1069. PMID 8109979. 
  5. "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. September 2002. doi:10.1104/pp.006544. PMID 12226526. 
  6. "Characterization of the constitutive and wound-inducible monoterpene cyclases of grand fir (Abies grandis)". Archives of Biochemistry and Biophysics 289 (2): 267–73. September 1991. doi:10.1016/0003-9861(91)90471-T. PMID 1898071. 
  7. "Wound-inducible pinene cyclase from grand fir: purification, characterization, and renaturation after SDS-PAGE". Archives of Biochemistry and Biophysics 293 (1): 167–73. February 1992. doi:10.1016/0003-9861(92)90380-f. PMID 1731633. 
  8. "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. August 1997. doi:10.1074/jbc.272.35.21784. PMID 9268308. 
  9. "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. July 2005. doi:10.1016/j.abb.2005.05.017. PMID 15978541. 
  10. "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. July 1995. doi:10.1016/0003-9861(95)90008-x. PMID 7625832. 
  11. "Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers". Archives of Biochemistry and Biophysics 372 (1): 197–204. December 1999. doi:10.1006/abbi.1999.1467. PMID 10562434. 
  12. "Insect attack and wounding induce traumatic resin duct development and gene expression of (-)-pinene synthase in Sitka spruce". Plant Physiology 133 (1): 368–78. September 2003. doi:10.1104/pp.103.022723. PMID 12970502. 

External links