Histidine residue at position 234 of oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae simultaneously influences cyclization, rearrangement, and deprotonation reactions

Tung-Kung Wu*, Yuan Ting Liu, Cheng Hsian Chang

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

Multiple triterpenes, including achilleol A (1), protosta-12,24-dien- 3β-ol (2), lanosterol (3), and parkeol (4; 14:26:51:9) were isolated from an ERG7 oxidosqualene-lanosterol cyclase-deficient Saccharomyces cerevisiae TKW14 strain that expresses the ERG7H234Y mutation. The results indicate a role for H234 in modulating multiple aspects of the oxidosqualene cyclization/rearrangement reaction, including cyclization, rearrangement, and deprotonation.

Original languageEnglish
Pages (from-to)1177-1181
Number of pages5
JournalChemBioChem
Volume6
Issue number7
DOIs
StatePublished - 1 Jul 2005

Keywords

  • Cyclization
  • Homology modeling
  • Oxidosqualene cyclase
  • Rearrangement
  • Sterols
  • Terpenoids

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