Abietadiene synthase

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In enzymology, an abietadiene synthase (EC 4.2.3.18) is an enzyme that catalyzes the chemical reaction

(+)-copalyl diphosphate $\rightleftharpoons$ (-)-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.

[edit] References

IUBMB entry for 4.2.3.18
BRENDA references for 4.2.3.18 (Recommended.)
PubMed references for 4.2.3.18
PubMed Central references for 4.2.3.18
Google Scholar references for 4.2.3.18
RB (2000). "Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the "pseudomature" recombinant enzyme". Biochemistry. 39: 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: 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: 580–4. doi:10.1073/pnas.022627099. PMID 11805316.
Peters RJ, Croteau RB (2002). "Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate". Biochemistry. 41: 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: 6998–7006. doi:10.1021/ja017734b. PMID 12059223.