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. 1968 Feb;106(3):659–665. doi: 10.1042/bj1060659

The biosynthesis of β-amyrin. Mechanism of squalene cyclization

H H Rees 1,*, G Britton 1,*, T W Goodwin 1,*
PMCID: PMC1198556  PMID: 5639923

Abstract

1. β-Amyrin synthesized by pea seedlings in the presence of (3RS)-[2-14C,(4R)-4-3H1]mevalonic acid (for nomenclature see Cahn, Ingold & Prelog, 1956) was subjected to a series of degradations to locate the positions within the molecule of the incorporated tritium. 2. The location of five of the six labelled hydrogen atoms at C-3, C-9, C-18 and C-19 (two) confirms that the mechanism of cyclization of squalene expected from the biogenetic isoprene rule is functioning in vivo.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Corey E. J., Ortiz de Montellano P. R. Enzymic synthesis of beta-amyrin from 2,3-oxidosqualene. J Am Chem Soc. 1967 Jun 21;89(13):3362–3363. doi: 10.1021/ja00989a055. [DOI] [PubMed] [Google Scholar]
  2. Cornforth J. W., Cornforth R. H., Donninger C., Popják G. Studies on the biosynthesis of cholesterol XIX. Steric course of hydrogen eliminations and of C-C bond formations in squalene biosynthesis. Proc R Soc Lond B Biol Sci. 1966 Jan 18;163(993):492–514. doi: 10.1098/rspb.1966.0004. [DOI] [PubMed] [Google Scholar]
  3. Rees H. H., Mercer E. I., Goodwin T. W. The stereospecific biosynthesis of plant sterols and alpha- and beta-amyrin. Biochem J. 1966 Jun;99(3):726–734. doi: 10.1042/bj0990726. [DOI] [PMC free article] [PubMed] [Google Scholar]

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