{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/87888"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/87888","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Kinetic Analysis and pH Dependence of the Phosphite Dehydrogenase Reaction","abstract":"The pH-rate profiles for active site mutants Lys76Ala, Glu266G1n, and Arg237Lys are also bell-shaped and the higher pKa of each is 8.4, which is also consistent with that observed for the pH dependence of sulfite inhibition for the wild type enzyme. Interestingly, the acidic limb of the Glu266Gln kcat/Km,HPt profile reveals a pKa of 7.2, which has been attributed to His292. A second variant, G1u266A1a, has a pH profile for kcat which is defined by a single pKa at 6.85 +/- 0.05 which also appears to be due to His292. The decrease in pKa for these mutants compared with the wild type indicates that a hydrogen bond exists between His292 and Glu266, and that interaction has been removed by replacing Glu266 with a neutral residue.","abstract_html":"The pH-rate profiles for active site mutants Lys76Ala, Glu266G1n, and Arg237Lys are also bell-shaped and the higher pKa of each is 8.4, which is also consistent with that observed for the pH dependence of sulfite inhibition for the wild type enzyme. Interestingly, the acidic limb of the Glu266Gln kcat/Km,HPt profile reveals a pKa of 7.2, which has been attributed to His292. A second variant, G1u266A1a, has a pH profile for kcat which is defined by a single pKa at 6.85 +/- 0.05 which also appears to be due to His292. The decrease in pKa for these mutants compared with the wild type indicates that a hydrogen bond exists between His292 and Glu266, and that interaction has been removed by replacing Glu266 with a neutral residue.","abstract_has_math":false,"creators":["Relyea, Heather Ann"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":null,"degree_department":null,"school":null,"contributors":["Wilfred Van Der Donk"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2006,"date_issued":"2006","date_published":"2006","updated_at":"2026-07-22T22:26:31Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3242970"],"render_values":[{"text":"(MiAaPQ)AAI3242970","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/87888","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Wilfred Van Der Donk"]},{"key":"dc:creator","label":"Author","values":["Relyea, Heather Ann"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2006","2015-09-28T21:57:27Z","10000-01-01"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"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/2142/87888","(MiAaPQ)AAI3242970"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The pH-rate profiles for active site mutants Lys76Ala, Glu266G1n, and Arg237Lys are also bell-shaped and the higher pKa of each is 8.4, which is also consistent with that observed for the pH dependence of sulfite inhibition for the wild type enzyme. Interestingly, the acidic limb of the Glu266Gln kcat/Km,HPt profile reveals a pKa of 7.2, which has been attributed to His292. A second variant, G1u266A1a, has a pH profile for kcat which is defined by a single pKa at 6.85 +/- 0.05 which also appears to be due to His292. The decrease in pKa for these mutants compared with the wild type indicates that a hydrogen bond exists between His292 and Glu266, and that interaction has been removed by replacing Glu266 with a neutral residue.","Made available in DSpace on 2015-09-28T21:57:27Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3242970.pdf: 2971025 bytes, checksum: 168192ba6678e41248a63eaa9efc9abd (MD5) Previous issue date: 2006","Embargo set by: Seth Robbins for item 89169 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","111 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2006."]},{"key":"dc:title","label":"Title","values":["Kinetic Analysis and pH Dependence of the Phosphite Dehydrogenase Reaction"]}]}],"canonical_facts":{"dc:contributor":["Wilfred Van Der Donk"],"dc:creator":["Relyea, Heather Ann"],"dc:date":["2006","2015-09-28T21:57:27Z","10000-01-01"],"dc:description":["The pH-rate profiles for active site mutants Lys76Ala, Glu266G1n, and Arg237Lys are also bell-shaped and the higher pKa of each is 8.4, which is also consistent with that observed for the pH dependence of sulfite inhibition for the wild type enzyme. Interestingly, the acidic limb of the Glu266Gln kcat/Km,HPt profile reveals a pKa of 7.2, which has been attributed to His292. A second variant, G1u266A1a, has a pH profile for kcat which is defined by a single pKa at 6.85 +/- 0.05 which also appears to be due to His292. The decrease in pKa for these mutants compared with the wild type indicates that a hydrogen bond exists between His292 and Glu266, and that interaction has been removed by replacing Glu266 with a neutral residue.","Made available in DSpace on 2015-09-28T21:57:27Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3242970.pdf: 2971025 bytes, checksum: 168192ba6678e41248a63eaa9efc9abd (MD5) Previous issue date: 2006","Embargo set by: Seth Robbins for item 89169 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","111 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2006."],"dc:identifier":["http://hdl.handle.net/2142/87888","(MiAaPQ)AAI3242970"],"dc:language":["eng"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["Kinetic Analysis and pH Dependence of the Phosphite Dehydrogenase Reaction"],"dc:type":["text"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:31Z"}