Copalyl diphosphate

Copalyl diphosphate is a lipid of Prenol Lipids (PR) class.

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Current reference collection contains 75 references associated with Copalyl diphosphate in LipidPedia. Due to lack of full text of references or no associated biomedical terms are recognized in our current text-mining method, we cannot extract any biomedical terms related to diseases, pathways, locations, functions, genes, lipids, and animal models from the associated reference collection.

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All references with Copalyl diphosphate

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Authors Title Published Journal PubMed Link
pmid:
Ravn MM et al. Stereochemistry of the cyclization-rearrangement of (+)-copalyl diphosphate to (-)-abietadiene catalyzed by recombinant abietadiene synthase from Abies grandis. 2000 Org. Lett. pmid:10814381
Peters RJ et al. Bifunctional abietadiene synthase: free diffusive transfer of the (+)-copalyl diphosphate intermediate between two distinct active sites. 2001 J. Am. Chem. Soc. pmid:11552804
Peters RJ and Croteau RB Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate. 2002 Biochemistry pmid:11827528
Ravn MM et al. Mechanism of abietadiene synthase catalysis: stereochemistry and stabilization of the cryptic pimarenyl carbocation intermediates. 2002 J. Am. Chem. Soc. pmid:12059223
Toshima H et al. Total synthesis of (+/-)-syn-copalol. 2002 Biosci. Biotechnol. Biochem. pmid:12506998
Peters RJ et al. Bifunctional abietadiene synthase: mutual structural dependence of the active sites for protonation-initiated and ionization-initiated cyclizations. 2003 Biochemistry pmid:12614165
Morrone D et al. Evident and latent plasticity across the rice diterpene synthase family with potential implications for the evolution of diterpenoid metabolism in the cereals. 2011 Biochem. J. pmid:21323642
Siebert MR et al. The need for enzymatic steering in abietic acid biosynthesis: gas-phase chemical dynamics simulations of carbocation rearrangements on a bifurcating potential energy surface. 2011 J. Am. Chem. Soc. pmid:21548620
Zerbe P et al. Mutational analysis of white spruce (Picea glauca) ent-kaurene synthase (PgKS) reveals common and distinct mechanisms of conifer diterpene synthases of general and specialized metabolism. 2012 Phytochemistry pmid:22177479

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