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Tryptophan 232 within Oxidosqualene-Lanosterol Cyclase from Saccharomyces cerevisiae Influences Rearrangement and Deprotonation but Not Cyclization Reactions.

Oxidosqualene-lanosterol cyclases convert oxidosqualene to lanosterol in yeast and mammals. Site-saturated mutants' construction of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase, at Trp232 exchanges against proteinogenic amino acids, and product profiles are shown. All mutants, except Lys and Arg, produced protosta-12,24-dien-3beta-ol, lanosterol, and parkeol. Overall, Trp232 plays a catalytic role in the influence of rearrangement process and determination of deprotonation position but does not involve intervention in the cyclization steps.[1]

References

  1. Tryptophan 232 within Oxidosqualene-Lanosterol Cyclase from Saccharomyces cerevisiae Influences Rearrangement and Deprotonation but Not Cyclization Reactions. Wu, T.K., Yu, M.T., Liu, Y.T., Chang, C.H., Wang, H.J., Diau, E.W. Org. Lett. (2006) [Pubmed]
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