{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84891"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84891","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Mechanistic Investigations of Mandelate Racemase: The Electrophilic Catalysts","abstract":"MR is a member of the enolase superfamily (Babbitt et al., 1996), which is a family of proteins which are both structurally and mechanistically related. All the family members have highly conserved metal ion ligands. Based on the homology to enolase, which requires two divalent metal ions, MR as well as other members of the enolase superfamily might require two metal ions. The stoichiometries of metal ion requirements for MR, muconate lactonizing enzyme (MLE), galactonate dehydratase (GalD) and glucarate dehydratase (GlucD) were determined. MR and MLE bind and require a single metal ion for activity. GalD and GlucD require two metals for activity and show inhibition at high metal ion concentrations with Mn$\\sp{2+}.$.","abstract_html":"MR is a member of the enolase superfamily (Babbitt et al., 1996), which is a family of proteins which are both structurally and mechanistically related. All the family members have highly conserved metal ion ligands. Based on the homology to enolase, which requires two divalent metal ions, MR as well as other members of the enolase superfamily might require two metal ions. The stoichiometries of metal ion requirements for MR, muconate lactonizing enzyme (MLE), galactonate dehydratase (GalD) and glucarate dehydratase (GlucD) were determined. MR and MLE bind and require a single metal ion for activity. GalD and GlucD require two metals for activity and show inhibition at high metal ion concentrations with Mn$\\sp{2+}.$.","abstract_has_math":true,"creators":["Budihas, Scott Ronald"],"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":"2015-09-25T22:28:22Z","date_published":"2015-09-25T22:28:22Z","updated_at":"2026-07-22T22:26:24Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9904398"],"render_values":[{"text":"(MiAaPQ)AAI9904398","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84891","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":["Budihas, Scott Ronald"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:28:22Z","10000-01-01","1998"]},{"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":["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/2142/84891","(MiAaPQ)AAI9904398"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["MR is a member of the enolase superfamily (Babbitt et al., 1996), which is a family of proteins which are both structurally and mechanistically related. All the family members have highly conserved metal ion ligands. Based on the homology to enolase, which requires two divalent metal ions, MR as well as other members of the enolase superfamily might require two metal ions. The stoichiometries of metal ion requirements for MR, muconate lactonizing enzyme (MLE), galactonate dehydratase (GalD) and glucarate dehydratase (GlucD) were determined. MR and MLE bind and require a single metal ion for activity. GalD and GlucD require two metals for activity and show inhibition at high metal ion concentrations with Mn$\\sp{2+}.$.","Made available in DSpace on 2015-09-25T22:28:22Z (GMT). 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All the family members have highly conserved metal ion ligands. Based on the homology to enolase, which requires two divalent metal ions, MR as well as other members of the enolase superfamily might require two metal ions. The stoichiometries of metal ion requirements for MR, muconate lactonizing enzyme (MLE), galactonate dehydratase (GalD) and glucarate dehydratase (GlucD) were determined. MR and MLE bind and require a single metal ion for activity. GalD and GlucD require two metals for activity and show inhibition at high metal ion concentrations with Mn$\\sp{2+}.$.","Made available in DSpace on 2015-09-25T22:28:22Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9904398.pdf: 4176447 bytes, checksum: 5ffce56c8d23d6723247aa6178f36947 (MD5) Previous issue date: 1998","Embargo set by: Seth Robbins for item 86172 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","110 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998."],"dc:identifier":["http://hdl.handle.net/2142/84891","(MiAaPQ)AAI9904398"],"dc:language":["eng"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["Mechanistic Investigations of Mandelate Racemase: The Electrophilic Catalysts"],"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":"2026-07-22T22:26:24Z"}