Histidine Residue at Position 234 of Oxidosqualene‐Lanosterol Cyclase from  Saccharomyces cerevisiae  Simultaneously Influences Cyclization, Rearrangement, and Deprotonation Reactions | Zendy

Wu TungKung | Zendy; Liu YuanTing | Zendy; Chang ChengHsian | Zendy

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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.

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