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Enzymatic Formation of Multiple Triterpenes by Mutation of Tyrosine 510 of the Oxidosqualene‐Lanosterol Cyclase from Saccharomyces cerevisiae
Author(s) -
Wu TungKung,
Chang ChengHsiang
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400079
Subject(s) - saccharomyces cerevisiae , lanosterol , stereochemistry , chemistry , deprotonation , enzyme , cyclase , terpene , biochemistry , tyrosine , residue (chemistry) , yeast , sterol , organic chemistry , ion , cholesterol
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.