{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/86735"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/86735","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Studies of Acetyl-Coa Carboxylase From Escherichia Coli","abstract":"Preliminary functional assignments for the two subunits in the carboxyltransferase complex have been given. The alpha subunit (AccA) appears to have a structural role in the total ACC complex while the beta subunit (AccD) could contain the carboxyltransferase active site. The above conclusions are based on enzymatic deactivational studies with extracts only overproducing AccBCD with and without PEG (14%) compared to extracts with all four subunits overproduced (AccABCD) for the assignment of the AccA function. Extracts only overproducing AccD contained higher carboxyltransferase activity leading one to conclude the active site for the complex is contained in the AccD subunit.","abstract_html":"Preliminary functional assignments for the two subunits in the carboxyltransferase complex have been given. The alpha subunit (AccA) appears to have a structural role in the total ACC complex while the beta subunit (AccD) could contain the carboxyltransferase active site. The above conclusions are based on enzymatic deactivational studies with extracts only overproducing AccBCD with and without PEG (14%) compared to extracts with all four subunits overproduced (AccABCD) for the assignment of the AccA function. Extracts only overproducing AccD contained higher carboxyltransferase activity leading one to conclude the active site for the complex is contained in the AccD subunit.","abstract_has_math":false,"creators":["Davis, Mark Stephen"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Cronan, John E., Jr"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-28T15:17:44Z","date_published":"2015-09-28T15:17:44Z","updated_at":"2026-07-22T22:26:27Z","subjects":["Biology, Molecular"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9912216"],"render_values":[{"text":"(MiAaPQ)AAI9912216","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/86735","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Cronan, John E., Jr"]},{"key":"dc:creator","label":"Author","values":["Davis, Mark Stephen"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-28T15:17:44Z","10000-01-01","1998"]},{"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/2142/86735","(MiAaPQ)AAI9912216"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Preliminary functional assignments for the two subunits in the carboxyltransferase complex have been given. The alpha subunit (AccA) appears to have a structural role in the total ACC complex while the beta subunit (AccD) could contain the carboxyltransferase active site. The above conclusions are based on enzymatic deactivational studies with extracts only overproducing AccBCD with and without PEG (14%) compared to extracts with all four subunits overproduced (AccABCD) for the assignment of the AccA function. Extracts only overproducing AccD contained higher carboxyltransferase activity leading one to conclude the active site for the complex is contained in the AccD subunit.","Made available in DSpace on 2015-09-28T15:17:44Z (GMT). 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The alpha subunit (AccA) appears to have a structural role in the total ACC complex while the beta subunit (AccD) could contain the carboxyltransferase active site. The above conclusions are based on enzymatic deactivational studies with extracts only overproducing AccBCD with and without PEG (14%) compared to extracts with all four subunits overproduced (AccABCD) for the assignment of the AccA function. Extracts only overproducing AccD contained higher carboxyltransferase activity leading one to conclude the active site for the complex is contained in the AccD subunit.","Made available in DSpace on 2015-09-28T15:17:44Z (GMT). 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