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dc.contributor.authorJustyn Wayne Jaworski-
dc.date.accessioned2017-11-07T04:49:42Z-
dc.date.available2017-11-07T04:49:42Z-
dc.date.issued2016-01-
dc.identifier.citationBIOCHEMICAL ENGINEERING JOURNAL, v. 105, Page. 446-454en_US
dc.identifier.issn1369-703X-
dc.identifier.issn1873-295X-
dc.identifier.urihttp://www.sciencedirect.com/science/article/pii/S1369703X15300930?via%3Dihub-
dc.identifier.urihttp://hdl.handle.net/20.500.11754/30530-
dc.description.abstractFormylglycine generating enzyme (FGE) is conserved through most organisms for the post-translational formation of aldehyde bearing formylglycine residues, often at sites possessing the general motif XCXPXRX. Using a library of the XCXPXRX repertoire displayed on the p3 protein coat of fd phage, we devised a phage screening strategy for identifying FGE substrates. Our methods of screening phage possessing possible substrates for enzymatic activity made use of the unique aldehyde residues produced on the substrate by reaction with FGE, which facilitated covalent capture of phage onto magnetic beads. This sequence dependent conversion/capture in conjunction with an unexpected sequence dependence of the-enzymatic elution step used to liberate the phage for propagation served as the evolutionary selection pressures. The resulting HCTPRRP sequence identified from this phage screening procedure was an effective substrate for FGE, and through the course of the screening process it was selected for its propensity to be cleaved by trypsin. We anticipate this unique methodology for enzyme substrate screening may be applicable to selection of novel enzyme-substrate pairs by virtue of either sequence dependent immobilization or sequence dependent elution. (C) 2015 Elsevier B.V. All rights reserved.en_US
dc.description.sponsorshipThis work was supported by the Basic Science Research Program through the National Research Foundation (NRF) funded by the Ministry of Science, ICT & Future Planning (2013R1A1A1076117) and also by the Priority Research Centers Program through the NRF funded by the Ministry of Education (2012R1A6A1029029).en_US
dc.language.isoenen_US
dc.publisherELSEVIER SCIENCE BVen_US
dc.subjectEnzymesen_US
dc.subjectProteinen_US
dc.subjectImmobilizationen_US
dc.subjectAmino acidsen_US
dc.subjectSubstrate screeningen_US
dc.subjectFilamentous bacteriophageen_US
dc.titlePhage based screening strategy for identifying enzyme substratesen_US
dc.typeArticleen_US
dc.relation.volume105-
dc.identifier.doi10.1016/j.bej.2015.10.022-
dc.relation.page446-454-
dc.relation.journalBIOCHEMICAL ENGINEERING JOURNAL-
dc.contributor.googleauthorCheok, Hui Shan-
dc.contributor.googleauthorJaworski, Justyn-
dc.relation.code2016002057-
dc.sector.campusS-
dc.sector.daehakCOLLEGE OF ENGINEERING[S]-
dc.sector.departmentDEPARTMENT OF CHEMICAL ENGINEERING-
dc.identifier.pidjustynj-
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COLLEGE OF ENGINEERING[S](공과대학) > CHEMICAL ENGINEERING(화학공학과) > Articles
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