Abstract
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-3β-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.
| Original language | English |
|---|---|
| Pages (from-to) | 1319-1322 |
| Number of pages | 4 |
| Journal | Organic Letters |
| Volume | 8 |
| Issue number | 7 |
| DOIs | |
| State | Published - 30 Mar 2006 |
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Wu, T-K., Yu, M. T., Liu, Y. T., Chang, C. H., Wang, H. J., & Diau, W-G. (2006). Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions. Organic Letters, 8(7), 1319-1322. https://doi.org/10.1021/ol053134w