Protein plasticity: A single amino acid substitution in the Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase generates protosta-13(17),24-dien- 3β-ol, a rearrangement product

Tung-Kung Wu*, Hao Yu Wen, Cheng Hsiang Chang, Yuan Ting Liu

*Corresponding author for this work

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

(Chemical Equation Presented) To provide insights into the structure-function relationships of oxidosqualene-lanosterol cyclase (ERG7) from Saccharomyces cerevisiae, the Phe699 was exchanged against hydrophilic polar uncharged residues Ser, Thr, Cys, Gln, and Tyr to characterize its product profile and functional role in ERG7 activity. Among the substitutions, only the ERG7F699T mutant produced novel protosta-13(17),24-dien-3β-ol as the sole truncated rearrangement product. The results suggest that Phe699Thr mutation is likely to affect the C-17 cation stabilization during the rearrangement process.

Original languageEnglish
Pages (from-to)2529-2532
Number of pages4
JournalOrganic Letters
Volume10
Issue number12
DOIs
StatePublished - 1 Dec 2008

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