Premium
Histidine Residue at Position 234 of Oxidosqualene‐Lanosterol Cyclase from Saccharomyces cerevisiae Simultaneously Influences Cyclization, Rearrangement, and Deprotonation Reactions
Author(s) -
Wu TungKung,
Liu YuanTing,
Chang ChengHsian
Publication year - 2005
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.200500084
Subject(s) - saccharomyces cerevisiae , lanosterol , deprotonation , stereochemistry , histidine , cope rearrangement , cyclase , chemistry , chatterjee , residue (chemistry) , biochemistry , yeast , sterol , computer science , amino acid , enzyme , organic chemistry , ion , cholesterol , bengali , artificial intelligence
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 ERG7 H234Y mutation. The results indicate a role for H234 in modulating multiple aspects of the oxidosqualene cyclization/rearrangement reaction, including cyclization, rearrangement, and deprotonation.