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Differential Stereocontrolled Formation of Tricyclic Triterpenes by Mutation of Tyrosine 99 of the Oxidosqualene-Lanosterol Cyclase from Saccharomyces cerevisiae

dc.citation.epage5737en_US
dc.citation.issue33en_US
dc.citation.spage5731en_US
dc.citation.volumeen_US
dc.citation.woscount9
dc.contributor.authorWu, Tung-Kungen_US
dc.contributor.authorLi, Wen-Hsuanen_US
dc.contributor.authorChang, Cheng-Hsiangen_US
dc.contributor.authorWen, Hao-Yuen_US
dc.contributor.authorLiu, Yuan-Tingen_US
dc.contributor.authorChang, Yi-Chunen_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.date.accessioned2014-12-08T15:08:25Z
dc.date.available2014-12-08T15:08:25Z
dc.date.issued2009-11-01en_US
dc.description.abstractThe function of the Tyr99 residue from Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase (ERG7) was analyzed by constructing deletion and site-saturated mutants. Two truncated intermediates, (13 alpha H)-isomalabarica-14Z,17E,21-trien-3 beta-ol and (13 alpha H)-isomalabarica-14E,17E,21-trien-3 beta-ol, were isolated from the ERG7(Y99X) mutants. These results suggest that the functional role of ERG7(Y99) is to affect both chair-boat 6-6-5 tricyclic Markovnikov C-14 cation stabilization and the stereochemistry of the protons at the C-15 position for subsequent deprotonation. ((C) Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009)en_US
dc.identifier.doi10.1002/ejoc.200900638en_US
dc.identifier.issn1434-193Xen_US
dc.identifier.journalEUROPEAN JOURNAL OF ORGANIC CHEMISTRYen_US
dc.identifier.urihttp://dx.doi.org/10.1002/ejoc.200900638en_US
dc.identifier.urihttps://ir.lib.nycu.edu.tw/handle/11536/6510
dc.identifier.wosnumberWOS:000272330600005
dc.language.isoen_USen_US
dc.subjectMutagenesisen_US
dc.subjectCyclizationen_US
dc.subjectEnzymesen_US
dc.subjectReaction mechanismsen_US
dc.subjectTerpenoidsen_US
dc.titleDifferential Stereocontrolled Formation of Tricyclic Triterpenes by Mutation of Tyrosine 99 of the Oxidosqualene-Lanosterol Cyclase from Saccharomyces cerevisiaeen_US
dc.typeArticleen_US

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