From Wikipedia, the free encyclopedia
(+)-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
Search
PMC articles
PubMed articles
NCBI proteins

(+)-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 (+)- α-pinene + diphosphate

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

References

  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  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. ^ 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.
  6. ^ 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

From Wikipedia, the free encyclopedia
(+)-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
Search
PMC articles
PubMed articles
NCBI proteins

(+)-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 (+)- α-pinene + diphosphate

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

References

  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  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. ^ 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.
  6. ^ 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


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