Phenylalanine 445 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae Influences C-ring cyclization and deprotonation reactions

Tung-Kung Wu*, Yuan Ting Liu, Feng Hsuan Chiu, Cheng Hsiang Chang

*Corresponding author for this work

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

(Chemical Equation Presented) We describe the Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase Phe445 site-saturated mutants that generate truncated tricyclic and altered deprotonation product profiles. Among these mutants, only polar side-chain group substitutions genetically complemented yeast viability and produced spatially related product diversity, supporting the Johnson model that cation-π interactions between a carbocationic intermediate and an enzyme can be replaced by an electrostatic or polar side chain to stabilize the cationic intermediate, but with product differentiation.

Original languageEnglish
Pages (from-to)4691-4694
Number of pages4
JournalOrganic Letters
Volume8
Issue number21
DOIs
StatePublished - 12 Oct 2006

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