{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84328"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84328","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Investigations of the Substrate Specificity of Lacticin 481 Synthetase and Utilization in Peptide Engineering Applications","abstract":"The promiscuous activity of LctM toward LctA prepeptides containing nonproteinogenic amino acids prompted the evaluation of LctM as a general catalyst for the introduction of post-translational modifications in non-lantibiotic peptides fused to the LctA leader peptide. LctM was utilized to efficiently introduce dehydrated, phosphorylated, and lanthionine cross-linked amino acids into therapeutically relevant non-lantibiotic peptides. Furthermore, enzymatically installed dehydro amino acids were used as sites of ligation with a variety of thiol nucleophiles for the preparation of peptide conjugates. Lastly, the role of the leader peptide in lacticin 481 biosynthesis was investigated. Surprisingly, the leader peptide was not required for dehydration activity of LctM, although it greatly enhanced the catalytic efficiency of LctM.","abstract_html":"The promiscuous activity of LctM toward LctA prepeptides containing nonproteinogenic amino acids prompted the evaluation of LctM as a general catalyst for the introduction of post-translational modifications in non-lantibiotic peptides fused to the LctA leader peptide. LctM was utilized to efficiently introduce dehydrated, phosphorylated, and lanthionine cross-linked amino acids into therapeutically relevant non-lantibiotic peptides. Furthermore, enzymatically installed dehydro amino acids were used as sites of ligation with a variety of thiol nucleophiles for the preparation of peptide conjugates. Lastly, the role of the leader peptide in lacticin 481 biosynthesis was investigated. Surprisingly, the leader peptide was not required for dehydration activity of LctM, although it greatly enhanced the catalytic efficiency of LctM.","abstract_has_math":false,"creators":["Levengood, Matthew"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["van der Donk, Wilfred A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:13:58Z","date_published":"2015-09-25T22:13:58Z","updated_at":"2026-07-22T22:26:23Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3347436"],"render_values":[{"text":"(MiAaPQ)AAI3347436","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84328","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["van der Donk, Wilfred A."]},{"key":"dc:creator","label":"Author","values":["Levengood, Matthew"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:13:58Z","10000-01-01","2008"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry, Biochemistry"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/84328","(MiAaPQ)AAI3347436"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The promiscuous activity of LctM toward LctA prepeptides containing nonproteinogenic amino acids prompted the evaluation of LctM as a general catalyst for the introduction of post-translational modifications in non-lantibiotic peptides fused to the LctA leader peptide. LctM was utilized to efficiently introduce dehydrated, phosphorylated, and lanthionine cross-linked amino acids into therapeutically relevant non-lantibiotic peptides. Furthermore, enzymatically installed dehydro amino acids were used as sites of ligation with a variety of thiol nucleophiles for the preparation of peptide conjugates. Lastly, the role of the leader peptide in lacticin 481 biosynthesis was investigated. Surprisingly, the leader peptide was not required for dehydration activity of LctM, although it greatly enhanced the catalytic efficiency of LctM.","Made available in DSpace on 2015-09-25T22:13:58Z (GMT). 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LctM was utilized to efficiently introduce dehydrated, phosphorylated, and lanthionine cross-linked amino acids into therapeutically relevant non-lantibiotic peptides. Furthermore, enzymatically installed dehydro amino acids were used as sites of ligation with a variety of thiol nucleophiles for the preparation of peptide conjugates. Lastly, the role of the leader peptide in lacticin 481 biosynthesis was investigated. Surprisingly, the leader peptide was not required for dehydration activity of LctM, although it greatly enhanced the catalytic efficiency of LctM.","Made available in DSpace on 2015-09-25T22:13:58Z (GMT). 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