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dc.contributor.authorChang, Keng-Mingen_US
dc.contributor.authorChen, Shih-Hsunen_US
dc.contributor.authorKuo, Chih-Jungen_US
dc.contributor.authorChang, Chi-Kangen_US
dc.contributor.authorGuo, Rey-Tingen_US
dc.contributor.authorYang, Jinn-Moonen_US
dc.contributor.authorLiang, Po-Huangen_US
dc.date.accessioned2014-12-08T15:22:42Z-
dc.date.available2014-12-08T15:22:42Z-
dc.date.issued2012-04-24en_US
dc.identifier.issn0006-2960en_US
dc.identifier.urihttp://hdl.handle.net/11536/16023-
dc.description.abstractOctaprenyl diphosphate synthase (OPPS) catalyzes consecutive condensation reactions of farnesyl diphosphate (FPP) with five molecules of isopentenyl diphosphates (IPP) to generate C-40 octaprenyl diphosphate, which constitutes the side chain of ubiquinone or menaquinone. To understand the roles of active site amino acids in substrate binding and catalysis, we conducted site-directed mutagenesis studies with Escherichia coli OPPS. In conclusion, D85 is the most important residue in the first DDXXD motif for both FPP and IPP binding through an H-bond network involving R93 and R94, respectively, whereas R94, K45, R48, and H77 are responsible for IPP binding by providing H-bonds and ionic interactions. K170 and T171 may stabilize the farnesyl carbocation intermediate to facilitate the reaction, whereas R93 and K225 may stabilize the catalytic base (MgPPi) for H-R proton abstraction after IPP condensation. K225 and K235 in a flexible loop may interact with FPP when the enzyme becomes a closed conformation, which is therefore crucial for catalysis. Q208 is near the hydrophobic part of IPP and is important for IPP binding and catalysis.en_US
dc.language.isoen_USen_US
dc.titleRoles of Amino Acids in the Escherichia coli Octaprenyl Diphosphate Synthase Active Site Probed by Structure-Guided Site-Directed Mutagenesisen_US
dc.typeArticleen_US
dc.identifier.journalBIOCHEMISTRYen_US
dc.citation.volume51en_US
dc.citation.issue16en_US
dc.citation.epage3412en_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.identifier.wosnumberWOS:000303097100010-
dc.citation.woscount6-
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