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dc.contributor.authorWu, Tung-Kungen_US
dc.contributor.authorLiu, Yuan-Tingen_US
dc.contributor.authorChiu, Feng-Hsuanen_US
dc.contributor.authorChang, Cheng-Hsiangen_US
dc.date.accessioned2014-12-08T15:15:38Z-
dc.date.available2014-12-08T15:15:38Z-
dc.date.issued2006-10-12en_US
dc.identifier.issn1523-7060en_US
dc.identifier.urihttp://dx.doi.org/10.1021/ol061549ren_US
dc.identifier.urihttp://hdl.handle.net/11536/11677-
dc.description.abstractWe describe the Saccharomyces cerevisiae oxidosqualene - lanosterol cyclase Phe445 site-saturated mutants that generate truncated tricyclic and altered deprotonation product profiles. Among these mutants, only polar side-chain group substitutions genetically complemented yeast viability and produced spatially related product diversity, supporting the Johnson model that cation - pi interactions between a carbocationic intermediate and an enzyme can be replaced by an electrostatic or polar side chain to stabilize the cationic intermediate, but with product differentiation.en_US
dc.language.isoen_USen_US
dc.titlePhenylalanine 445 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences C-ring cyclization and deprotonation reactionsen_US
dc.typeArticleen_US
dc.identifier.doi10.1021/ol061549ren_US
dc.identifier.journalORGANIC LETTERSen_US
dc.citation.volume8en_US
dc.citation.issue21en_US
dc.citation.spage4691en_US
dc.citation.epage4694en_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.identifier.wosnumberWOS:000241030900006-
dc.citation.woscount16-
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