Importance of Saccharomyces cerevisiae Oxidosqualene-Lanosterol Cyclase Tyrosine 707 Residue for Chair-Boat Bicyclic Ring Formation and Deprotonation Reactions
| dc.citation.epage | 4962 | en_US |
| dc.citation.issue | 21 | en_US |
| dc.citation.spage | 4959 | en_US |
| dc.citation.volume | 10 | en_US |
| dc.citation.woscount | 14 | |
| dc.contributor.author | Wu, Tung-Kung | en_US |
| dc.contributor.author | Wang, Tsai-Ting | en_US |
| dc.contributor.author | Chang, Cheng-Hsiang | en_US |
| dc.contributor.author | Liu, Yuan-Ting | en_US |
| dc.contributor.author | Shie, Wen-Shiang | en_US |
| dc.contributor.department | 生物科技學系 | zh_TW |
| dc.contributor.department | Department of Biological Science and Technology | en_US |
| dc.date.accessioned | 2014-12-08T15:10:40Z | |
| dc.date.available | 2014-12-08T15:10:40Z | |
| dc.date.issued | 2008-11-06 | en_US |
| dc.description.abstract | A contact mapping strategy was applied to identity putative amino acid residues that influence the oxidosqualene-lanosterol B-ring cyclization reaction. A bicyclic intermediate with two altered deprotonation products, in conjunction with lanosterol, were isolated from the ERG7(Y707X) mutants, indicating that the Tyr707 residue may play a functional role in stabilizing the chair-boat bicyclic C-8 cation and the lanosteryl C-8/C-9 cation intermediates. | en_US |
| dc.identifier.doi | 10.1021/ol802036c | en_US |
| dc.identifier.issn | 1523-7060 | en_US |
| dc.identifier.journal | ORGANIC LETTERS | en_US |
| dc.identifier.uri | http://dx.doi.org/10.1021/ol802036c | en_US |
| dc.identifier.uri | https://ir.lib.nycu.edu.tw/handle/11536/8159 | |
| dc.identifier.wosnumber | WOS:000260534500063 | |
| dc.language.iso | en_US | en_US |
| dc.title | Importance of Saccharomyces cerevisiae Oxidosqualene-Lanosterol Cyclase Tyrosine 707 Residue for Chair-Boat Bicyclic Ring Formation and Deprotonation Reactions | en_US |
| dc.type | Article | en_US |