Enzymatic formation of multiple triterpenes by mutation of tyrosine 510 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae

Tung-Kung Wu*, Cheng Hsiang Chang

*Corresponding author for this work

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

The simultaneous formation of monocyclic and differentially deprotonated triterpenes by mutation of Tyr510 of the oxidosqualene-lanosterol cyclase (ERG7) from Saccharomyces cerevisiae is reported (see scheme). Possible dual functions of this residue involved in the cyclization and deprotonation steps of the oxidosqualene cyclization/rearrangement cascade are discussed.

Original languageEnglish
Pages (from-to)1712-1715
Number of pages4
JournalChemBioChem
Volume5
Issue number12
DOIs
StatePublished - 31 Dec 2004

Keywords

  • Cyclization
  • Mutagenesis
  • Plasmid shuffle
  • Sterols
  • Terpenoids

Fingerprint Dive into the research topics of 'Enzymatic formation of multiple triterpenes by mutation of tyrosine 510 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae'. Together they form a unique fingerprint.

  • Cite this