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dc.contributor.authorWu, Tung-Kungen_US
dc.contributor.authorWang, Tsai-Tingen_US
dc.contributor.authorChang, Cheng-Hsiangen_US
dc.contributor.authorLiu, Yuan-Tingen_US
dc.contributor.authorShie, Wen-Shiangen_US
dc.date.accessioned2014-12-08T15:10:40Z-
dc.date.available2014-12-08T15:10:40Z-
dc.date.issued2008-11-06en_US
dc.identifier.issn1523-7060en_US
dc.identifier.urihttp://dx.doi.org/10.1021/ol802036cen_US
dc.identifier.urihttp://hdl.handle.net/11536/8159-
dc.description.abstractA 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.language.isoen_USen_US
dc.titleImportance of Saccharomyces cerevisiae Oxidosqualene-Lanosterol Cyclase Tyrosine 707 Residue for Chair-Boat Bicyclic Ring Formation and Deprotonation Reactionsen_US
dc.typeArticleen_US
dc.identifier.doi10.1021/ol802036cen_US
dc.identifier.journalORGANIC LETTERSen_US
dc.citation.volume10en_US
dc.citation.issue21en_US
dc.citation.spage4959en_US
dc.citation.epage4962en_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.identifier.wosnumberWOS:000260534500063-
dc.citation.woscount14-
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