{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84344"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84344","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Investigation of the Enzymes Involved in Lantibiotic Biosynthesis: Lacticin 481 and Haloduracin","abstract":"Finally, removal of the leader peptide from the modified precursor peptides is the final step in the maturation of lantibiotics, and is required for achievement of full biological activity. In lacticin 481 maturation, this peptide cleavage reaction is performed by the N-terminal protease domain of the lacticin 481 transporter, LctT. The activity of the protease domain of LctT was reconstituted in vitro and its substrate specificity was probed with numerous variants of the lacticin 481 precursor peptide. The N-terminal 150 amino acids of LctT were able to process most LctA mutant peptides, with the exception of peptides containing mutations at the double glycine motif located at the junction between leader sequence and structural region. Cys protease activity was confirmed for LctT as mutation of Cys12 to Ser or Ala abolished protease activity.","abstract_html":"Finally, removal of the leader peptide from the modified precursor peptides is the final step in the maturation of lantibiotics, and is required for achievement of full biological activity. In lacticin 481 maturation, this peptide cleavage reaction is performed by the N-terminal protease domain of the lacticin 481 transporter, LctT. The activity of the protease domain of LctT was reconstituted in vitro and its substrate specificity was probed with numerous variants of the lacticin 481 precursor peptide. The N-terminal 150 amino acids of LctT were able to process most LctA mutant peptides, with the exception of peptides containing mutations at the double glycine motif located at the junction between leader sequence and structural region. Cys protease activity was confirmed for LctT as mutation of Cys12 to Ser or Ala abolished protease activity.","abstract_has_math":false,"creators":["Ihnken, Leigh Anne Furgerson"],"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":"2015-09-25T22:14:02Z","date_published":"2015-09-25T22:14:02Z","updated_at":"2026-07-22T22:26:23Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3392075"],"render_values":[{"text":"(MiAaPQ)AAI3392075","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84344","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":["Ihnken, Leigh Anne Furgerson"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:14:02Z","10000-01-01","2009"]},{"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/2142/84344","(MiAaPQ)AAI3392075"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Finally, removal of the leader peptide from the modified precursor peptides is the final step in the maturation of lantibiotics, and is required for achievement of full biological activity. In lacticin 481 maturation, this peptide cleavage reaction is performed by the N-terminal protease domain of the lacticin 481 transporter, LctT. The activity of the protease domain of LctT was reconstituted in vitro and its substrate specificity was probed with numerous variants of the lacticin 481 precursor peptide. The N-terminal 150 amino acids of LctT were able to process most LctA mutant peptides, with the exception of peptides containing mutations at the double glycine motif located at the junction between leader sequence and structural region. Cys protease activity was confirmed for LctT as mutation of Cys12 to Ser or Ala abolished protease activity.","Made available in DSpace on 2015-09-25T22:14:02Z (GMT). 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In lacticin 481 maturation, this peptide cleavage reaction is performed by the N-terminal protease domain of the lacticin 481 transporter, LctT. The activity of the protease domain of LctT was reconstituted in vitro and its substrate specificity was probed with numerous variants of the lacticin 481 precursor peptide. The N-terminal 150 amino acids of LctT were able to process most LctA mutant peptides, with the exception of peptides containing mutations at the double glycine motif located at the junction between leader sequence and structural region. Cys protease activity was confirmed for LctT as mutation of Cys12 to Ser or Ala abolished protease activity.","Made available in DSpace on 2015-09-25T22:14:02Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3392075.pdf: 2113071 bytes, checksum: 22edbc2920de44980bb902dcc2c02494 (MD5) Previous issue date: 2009","Embargo set by: Seth Robbins for item 85625 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","140 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2009."],"dc:identifier":["http://hdl.handle.net/2142/84344","(MiAaPQ)AAI3392075"],"dc:language":["eng"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["Investigation of the Enzymes Involved in Lantibiotic Biosynthesis: Lacticin 481 and Haloduracin"],"dc:type":["text"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:23Z"}