{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84902"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84902","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Galactonate Dehydratase: Exploring the Frontiers of the Enolase Superfamily","abstract":"The crystal structure of GalD indicates that His 185 may serve as a general acid catalyst to facilitate the departure of the 3-OH leaving group and/or stereospecifically protonate the product in the subsequent tautomerization reaction. The function of His 185 was investigated by comparing the kinetics of wild type, H285N, E310Q, H185Q and H185N GalD mutants, using both D-galactonate and 3-fluoro-3-deoxy-galactonate (F-Gal) as substrates. The kcat values for all the mutants decreased with D-galactonate, but only the kcat values for H185Q and H185N were relatively unaffected with F-Gal. Solvent deuterium incorporation studies with H185Q and H185N indicated that deuterium is stereospecifically protonated at the pro-S position. Thus, His 185 is involved in the beta-elimination of 3-OH but does not protonate the product in the subsequent tautomerization reaction.","abstract_html":"The crystal structure of GalD indicates that His 185 may serve as a general acid catalyst to facilitate the departure of the 3-OH leaving group and/or stereospecifically protonate the product in the subsequent tautomerization reaction. The function of His 185 was investigated by comparing the kinetics of wild type, H285N, E310Q, H185Q and H185N GalD mutants, using both D-galactonate and 3-fluoro-3-deoxy-galactonate (F-Gal) as substrates. The kcat values for all the mutants decreased with D-galactonate, but only the kcat values for H185Q and H185N were relatively unaffected with F-Gal. Solvent deuterium incorporation studies with H185Q and H185N indicated that deuterium is stereospecifically protonated at the pro-S position. Thus, His 185 is involved in the beta-elimination of 3-OH but does not protonate the product in the subsequent tautomerization reaction.","abstract_has_math":false,"creators":["Wieczorek, Stacey Jean"],"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":"2015-09-25T22:28:25Z","date_published":"2015-09-25T22:28:25Z","updated_at":"2026-07-22T22:26:24Z","subjects":["Chemistry, Organic"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9921753"],"render_values":[{"text":"(MiAaPQ)AAI9921753","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84902","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":["Wieczorek, Stacey Jean"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:28:25Z","10000-01-01","1999"]},{"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, Organic"]}]},{"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/2142/84902","(MiAaPQ)AAI9921753"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The crystal structure of GalD indicates that His 185 may serve as a general acid catalyst to facilitate the departure of the 3-OH leaving group and/or stereospecifically protonate the product in the subsequent tautomerization reaction. The function of His 185 was investigated by comparing the kinetics of wild type, H285N, E310Q, H185Q and H185N GalD mutants, using both D-galactonate and 3-fluoro-3-deoxy-galactonate (F-Gal) as substrates. The kcat values for all the mutants decreased with D-galactonate, but only the kcat values for H185Q and H185N were relatively unaffected with F-Gal. Solvent deuterium incorporation studies with H185Q and H185N indicated that deuterium is stereospecifically protonated at the pro-S position. Thus, His 185 is involved in the beta-elimination of 3-OH but does not protonate the product in the subsequent tautomerization reaction.","Made available in DSpace on 2015-09-25T22:28:25Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9921753.pdf: 5463079 bytes, checksum: 8032e7e916648e941f4069e1d8f9edd2 (MD5) Previous issue date: 1999","Embargo set by: Seth Robbins for item 86183 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","151 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1999."]},{"key":"dc:title","label":"Title","values":["Galactonate Dehydratase: Exploring the Frontiers of the Enolase Superfamily"]}]}],"canonical_facts":{"dc:contributor":["Gerlt, John A."],"dc:creator":["Wieczorek, Stacey Jean"],"dc:date":["2015-09-25T22:28:25Z","10000-01-01","1999"],"dc:description":["The crystal structure of GalD indicates that His 185 may serve as a general acid catalyst to facilitate the departure of the 3-OH leaving group and/or stereospecifically protonate the product in the subsequent tautomerization reaction. The function of His 185 was investigated by comparing the kinetics of wild type, H285N, E310Q, H185Q and H185N GalD mutants, using both D-galactonate and 3-fluoro-3-deoxy-galactonate (F-Gal) as substrates. The kcat values for all the mutants decreased with D-galactonate, but only the kcat values for H185Q and H185N were relatively unaffected with F-Gal. Solvent deuterium incorporation studies with H185Q and H185N indicated that deuterium is stereospecifically protonated at the pro-S position. Thus, His 185 is involved in the beta-elimination of 3-OH but does not protonate the product in the subsequent tautomerization reaction.","Made available in DSpace on 2015-09-25T22:28:25Z (GMT). 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