{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84776"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84776","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Methylmalonyl -Coa Decarboxylase (Ygfg) for Escherichia Coli: A New Activity for the Crotonase Superfamily","abstract":"The E113Q mutant exhibited significantly larger isotope effect for both kcat and kcat/Km than wild-type, suggesting differences in reaction mechanism between wild type and E113Q. Although experimental difficulties encountered did not allow quantitative studies of stereochemistry of the MMDC reaction, the reaction catalyzed by wild-type MMDC proceeds with retention of configuration using (S)-methylmalonyl-CoA as a substrate, and with inversion of configuration using (R)-methylmalonyl-CoA as a substrate. H66F catalyzed the MMDC reaction with at least partial racemization. I postulated that His66 is important in retaining structure of the active site.","abstract_html":"The E113Q mutant exhibited significantly larger isotope effect for both kcat and kcat/Km than wild-type, suggesting differences in reaction mechanism between wild type and E113Q. Although experimental difficulties encountered did not allow quantitative studies of stereochemistry of the MMDC reaction, the reaction catalyzed by wild-type MMDC proceeds with retention of configuration using (S)-methylmalonyl-CoA as a substrate, and with inversion of configuration using (R)-methylmalonyl-CoA as a substrate. H66F catalyzed the MMDC reaction with at least partial racemization. I postulated that His66 is important in retaining structure of the active site.","abstract_has_math":false,"creators":["Haller, Toomas"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Gerlt, John A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:27:50Z","date_published":"2015-09-25T22:27:50Z","updated_at":"2026-07-22T22:26:23Z","subjects":["Biology, Microbiology"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3023070"],"render_values":[{"text":"(MiAaPQ)AAI3023070","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84776","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Gerlt, John A."]},{"key":"dc:creator","label":"Author","values":["Haller, Toomas"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:27:50Z","10000-01-01","2001"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"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, Microbiology"]}]},{"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/2142/84776","(MiAaPQ)AAI3023070"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The E113Q mutant exhibited significantly larger isotope effect for both kcat and kcat/Km than wild-type, suggesting differences in reaction mechanism between wild type and E113Q. Although experimental difficulties encountered did not allow quantitative studies of stereochemistry of the MMDC reaction, the reaction catalyzed by wild-type MMDC proceeds with retention of configuration using (S)-methylmalonyl-CoA as a substrate, and with inversion of configuration using (R)-methylmalonyl-CoA as a substrate. H66F catalyzed the MMDC reaction with at least partial racemization. I postulated that His66 is important in retaining structure of the active site.","Made available in DSpace on 2015-09-25T22:27:50Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3023070.pdf: 9796868 bytes, checksum: a1905793dc00dee2c26cbf098e5da6c4 (MD5) Previous issue date: 2001","Embargo set by: Seth Robbins for item 86057 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","192 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2001."]},{"key":"dc:title","label":"Title","values":["Methylmalonyl -Coa Decarboxylase (Ygfg) for Escherichia Coli: A New Activity for the Crotonase Superfamily"]}]}],"canonical_facts":{"dc:contributor":["Gerlt, John A."],"dc:creator":["Haller, Toomas"],"dc:date":["2015-09-25T22:27:50Z","10000-01-01","2001"],"dc:description":["The E113Q mutant exhibited significantly larger isotope effect for both kcat and kcat/Km than wild-type, suggesting differences in reaction mechanism between wild type and E113Q. Although experimental difficulties encountered did not allow quantitative studies of stereochemistry of the MMDC reaction, the reaction catalyzed by wild-type MMDC proceeds with retention of configuration using (S)-methylmalonyl-CoA as a substrate, and with inversion of configuration using (R)-methylmalonyl-CoA as a substrate. H66F catalyzed the MMDC reaction with at least partial racemization. I postulated that His66 is important in retaining structure of the active site.","Made available in DSpace on 2015-09-25T22:27:50Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3023070.pdf: 9796868 bytes, checksum: a1905793dc00dee2c26cbf098e5da6c4 (MD5) Previous issue date: 2001","Embargo set by: Seth Robbins for item 86057 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","192 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2001."],"dc:identifier":["http://hdl.handle.net/2142/84776","(MiAaPQ)AAI3023070"],"dc:language":["eng"],"dc:subject":["Biology, Microbiology"],"dc:title":["Methylmalonyl -Coa Decarboxylase (Ygfg) for Escherichia Coli: A New Activity for the Crotonase Superfamily"],"dc:type":["text"],"thesis:degree_discipline":["Biochemistry"],"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"}