Abietadiene synthase
In enzymology, an abietadiene synthase (EC 4.2.3.18) is an enzyme that catalyzes the chemical reaction
- (+)-copalyl diphosphate (-)-abietadiene + diphosphate
Hence, this enzyme has one substrate, (+)-copalyl diphosphate, and two products, (-)-abietadiene and diphosphate.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is (+)-copalyl-diphosphate diphosphate-lyase [cyclizing (-)-abietadiene-forming]. This enzyme is also called copalyl-diphosphate diphosphate-lyase (cyclizing). This enzyme participates in diterpenoid biosynthesis.
References
- RB; Flory, JE; Jetter, R; Ravn, MM; Lee, HJ; Coates, RM; Croteau, RB (2000). "Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the "pseudomature" recombinant enzyme". Biochemistry. 39 (50): 15592–602. doi:10.1021/bi001997l. PMID 11112547.
- Peters RJ, Ravn MM, Coates RM, Croteau RB (2001). "Bifunctional abietadiene synthase: free diffusive transfer of the (+)-copalyl diphosphate intermediate between two distinct active sites". J. Am. Chem. Soc. 123 (37): 8974–8. doi:10.1021/ja010670k. PMID 11552804.
- Peters RJ, Croteau RB (2002). "Abietadiene synthase catalysis: mutational analysis of a prenyl diphosphate ionization-initiated cyclization and rearrangement". Proc. Natl. Acad. Sci. U. S. A. 99 (2): 580–4. doi:10.1073/pnas.022627099. PMC 117348. PMID 11805316. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=117348.
- Peters RJ, Croteau RB (2002). "Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate". Biochemistry. 41 (6): 1836–42. doi:10.1021/bi011879d. PMID 11827528.
- Ravn MM, Peters RJ, Coates RM, Croteau R (2002). "Mechanism of abietadiene synthase catalysis: stereochemistry and stabilization of the cryptic pimarenyl carbocation intermediates". J. Am. Chem. Soc. 124 (24): 6998–7006. doi:10.1021/ja017734b. PMID 12059223.