Biology:(+)-alpha-pinene synthase

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Short description: Class of enzymes
(+)-α-pinene synthase
Identifiers
EC number4.2.3.121
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

(+)-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

geranyl diphosphate [math]\displaystyle{ \rightleftharpoons }[/math] (+)-α-pinene + diphosphate

Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-α-pinene and (+)-camphene.

References

  1. "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. January 1984. PMID 6693393. 
  2. "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. 
  3. "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. February 1994. doi:10.1006/abbi.1994.1068. PMID 8109978. 
  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. "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. 
  6. "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. March 2003. doi:10.1016/s0003-9861(02)00746-4. PMID 12623076. 

External links