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dc.contributor.authorWu, TKen_US
dc.contributor.authorYu, MTen_US
dc.contributor.authorLiu, YTen_US
dc.contributor.authorChang, CHen_US
dc.contributor.authorWang, HJen_US
dc.contributor.authorDiau, EWGen_US
dc.date.accessioned2014-12-08T15:17:02Z-
dc.date.available2014-12-08T15:17:02Z-
dc.date.issued2006-03-30en_US
dc.identifier.issn1523-7060en_US
dc.identifier.urihttp://dx.doi.org/10.1021/ol053134wen_US
dc.identifier.urihttp://hdl.handle.net/11536/12470-
dc.description.abstractOxidosqualene-lanosterol cyclases convert oxidosqualene to lanosterol in yeast and mammals. Site-saturated mutants' construction of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase, at Trp232 exchanges against proteinogenic amino acids, and product profiles are shown. All mutants, except Lys and Arg, produced protosta-12,24-dien-3 beta-ol, lanosterol, and parkeol. Overall, Trp232 plays a catalytic role in the influence of rearrangement process and determination of deprotonation position but does not involve intervention in the cyclization steps.en_US
dc.language.isoen_USen_US
dc.titleTryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactionsen_US
dc.typeArticleen_US
dc.identifier.doi10.1021/ol053134wen_US
dc.identifier.journalORGANIC LETTERSen_US
dc.citation.volume8en_US
dc.citation.issue7en_US
dc.citation.spage1319en_US
dc.citation.epage1322en_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.department應用化學系zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.contributor.departmentDepartment of Applied Chemistryen_US
dc.identifier.wosnumberWOS:000236397000017-
dc.citation.woscount17-
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