Abstract
Squalene occupies a key position in the biosynthetic sequence from acetate to ergosterol (Fig. 1), being the first lipophilic intermediate in the pathway. The conversion of this 30-carbon hydrocarbon to the tetracyclic lanosterol structure was originally thought to occur in one step without intermediates. Tchen and Bloch (1957) showed that rat liver extracts require oxygen and reduced pyridine nucleotide to perform cyclisation of squalene. Yeast cells were also shown to require oxygen for ergosterol biosynthesis (Andreasen and Stier 1953) and to accumulate squalene under anaerobic conditions (Klein 1955). Subsequently, the intermediate 2,3-oxidosqualene was discovered (Corey et al. 1966; Van Tamelen et al. 1966) and squalene is now known to be converted by a two-step sequence of epoxidation and subsequent cyclisation involving two separate enzymes. The first of these enzymes, squalene epoxidase (EC 1.14.99.7), was initially described by Yamamoto and Bloch (1970) using rat liver extracts.
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Ryder, N.S. (1990). Squalene Epoxidase — Enzymology and Inhibition. In: Kuhn, P.J., Trinci, A.P.J., Jung, M.J., Goosey, M.W., Copping, L.G. (eds) Biochemistry of Cell Walls and Membranes in Fungi. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-74215-6_13
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DOI: https://doi.org/10.1007/978-3-642-74215-6_13
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