完整後設資料紀錄
DC 欄位語言
dc.contributor.authorHuang, Gou-Taoen_US
dc.contributor.authorYu, Jen-Shiang K.en_US
dc.date.accessioned2018-08-21T05:53:02Z-
dc.date.available2018-08-21T05:53:02Z-
dc.date.issued2017-12-01en_US
dc.identifier.issn2155-5435en_US
dc.identifier.urihttp://dx.doi.org/10.1021/acscata1.7b03398en_US
dc.identifier.urihttp://hdl.handle.net/11536/144191-
dc.description.abstractThe retro-aldol reaction catalyzed by pyruvate class II aldolase is investigated with QM/MM metadynamics; this enzyme transforms the substrate of 4-hydrox-y-2-ketoacid into pyruvate and aldehyde through the aldol cleavage. The hydroxyl group of the substrate is deprotonated by His45 with the aid of the metal-bound water, while the metal-bound hydroxide proposed in the literature is observed as a transient species. The deprotonation appears to enhance substrate binding between the deprotonated substrate and the active site. The reactive alkoxide is further stabilized by the salt bridge of Arg70-Asp42, facilitating the following aldol cleavage. The simulations show that the C-C bond cleavage is the rate-determining step, and the calculated barrier of approximately 14 kcal mol(-1) agrees reasonably with experimental data.en_US
dc.language.isoen_USen_US
dc.subjectaldol cleavageen_US
dc.subjectsalt bridgeen_US
dc.subjectaldolaseen_US
dc.subjectpyruvateen_US
dc.subjectQM/MMen_US
dc.subjectmetadynamicsen_US
dc.titleCatalytic Roles of Histidine and Arginine in Pyruvate Class II Aldolase: A Perspective from QM/MM Metadynamicsen_US
dc.typeArticleen_US
dc.identifier.doi10.1021/acscata1.7b03398en_US
dc.identifier.journalACS CATALYSISen_US
dc.citation.volume7en_US
dc.citation.spage8130en_US
dc.citation.epage8133en_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.department生物資訊及系統生物研究所zh_TW
dc.contributor.department分子醫學與生物工程研究所zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.contributor.departmentInstitude of Bioinformatics and Systems Biologyen_US
dc.contributor.departmentInstitute of Molecular Medicine and Bioengineeringen_US
dc.identifier.wosnumberWOS:000417230500011en_US
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