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dc.contributor.authorWu, Tung-Kungen_US
dc.contributor.authorWen, Hao-Yuen_US
dc.contributor.authorChang, Cheng-Hsiangen_US
dc.contributor.authorLiu, Yuan-Tingen_US
dc.date.accessioned2014-12-08T15:11:21Z-
dc.date.available2014-12-08T15:11:21Z-
dc.date.issued2008-06-19en_US
dc.identifier.issn1523-7060en_US
dc.identifier.urihttp://dx.doi.org/10.1021/ol800799nen_US
dc.identifier.urihttp://hdl.handle.net/11536/8711-
dc.description.abstractTo provide insights into the structure-function relationships of oxidosqualene-lanosterol cyclase (ERG7) from Saccharomyces cerevisiae, the Phe699 was exchanged against hydrophilic polar uncharged residues Ser, Thr, Cys, Gin, and Tyr to characterize its product profile and functional role in ERG7 activity. Among the substitutions, only the ERG7(F699T) mutant produced novel protosta-13(17),24-dien-3 beta-ol as the sole truncated rearrangement product. The results suggest that Phe699Thr mutation is likely to affect the C-17 cation stabilization during the rearrangement process.en_US
dc.language.isoen_USen_US
dc.titleProtein plasticity: A single amino acid substitution in the Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase generates protosta-13(17),24-dien-3 beta-ol, a rearrangement producten_US
dc.typeArticleen_US
dc.identifier.doi10.1021/ol800799nen_US
dc.identifier.journalORGANIC LETTERSen_US
dc.citation.volume10en_US
dc.citation.issue12en_US
dc.citation.spage2529en_US
dc.citation.epage2532en_US
dc.contributor.department應用化學系zh_TW
dc.contributor.department應用化學系分子科學碩博班zh_TW
dc.contributor.departmentDepartment of Applied Chemistryen_US
dc.contributor.departmentInstitute of Molecular scienceen_US
dc.identifier.wosnumberWOS:000256762100051-
dc.citation.woscount16-
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