{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/86629"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/86629","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"The prlC Suppressor Phenotype and Its Relation to Oligopeptidase a Specificity","abstract":"Comparisons of the prlC mutations with the crystal structure of Neurolysin reveal that the mutations are clustered in regions which are believed to affect access of substrates to the active site, not the active site itself. The prlC mutations may allow previously-restricted substrates to present their N-termini to the active site of OpdA. Because the PrlC mutant proteins suppress many different signal peptide mutations with no changes in the active site of OpdA, it is likely that wildtype OpdA also recognizes substrates of different lengths and sequences.","abstract_html":"Comparisons of the prlC mutations with the crystal structure of Neurolysin reveal that the mutations are clustered in regions which are believed to affect access of substrates to the active site, not the active site itself. The prlC mutations may allow previously-restricted substrates to present their N-termini to the active site of OpdA. Because the PrlC mutant proteins suppress many different signal peptide mutations with no changes in the active site of OpdA, it is likely that wildtype OpdA also recognizes substrates of different lengths and sequences.","abstract_has_math":false,"creators":["Flores, Theresa M."],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Miller, Charles G."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-28T15:17:02Z","date_published":"2015-09-28T15:17:02Z","updated_at":"2026-07-22T22:26:27Z","subjects":["Biology, Molecular"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3023057"],"render_values":[{"text":"(MiAaPQ)AAI3023057","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/86629","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Miller, Charles G."]},{"key":"dc:creator","label":"Author","values":["Flores, Theresa M."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-28T15:17:02Z","10000-01-01","2001"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology"]},{"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":["Biology, Molecular"]}]},{"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/2142/86629","(MiAaPQ)AAI3023057"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Comparisons of the prlC mutations with the crystal structure of Neurolysin reveal that the mutations are clustered in regions which are believed to affect access of substrates to the active site, not the active site itself. The prlC mutations may allow previously-restricted substrates to present their N-termini to the active site of OpdA. Because the PrlC mutant proteins suppress many different signal peptide mutations with no changes in the active site of OpdA, it is likely that wildtype OpdA also recognizes substrates of different lengths and sequences.","Made available in DSpace on 2015-09-28T15:17:02Z (GMT). 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The prlC mutations may allow previously-restricted substrates to present their N-termini to the active site of OpdA. Because the PrlC mutant proteins suppress many different signal peptide mutations with no changes in the active site of OpdA, it is likely that wildtype OpdA also recognizes substrates of different lengths and sequences.","Made available in DSpace on 2015-09-28T15:17:02Z (GMT). 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