{"id":{"repo_id":"buffalo","oai_identifier":"oai:ubir.buffalo.edu:10477/79853"},"canonical_url":"https://search.dev.ndltd.org/etd/buffalo/oai:ubir.buffalo.edu:10477/79853","repository":{"repo_id":"buffalo","name":"Buffalo","base_url":"https://ubir.buffalo.edu/oai/request"},"display":{"title":"Enzyme Architecture: The Role of a Flexible Loop in Activation of Glycerol-3-phosphate Dehydrogenase-Catalyzed Hydride Transfer","abstract":"M.S.","abstract_html":"M.S.","abstract_has_math":false,"creators":["He, Rui"],"institution":"State University of New York at Buffalo","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Richard, John","Chemistry"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2019,"date_issued":"2019-07-30T15:10:30Z","date_published":"2019-07-30T15:10:30Z","updated_at":"2026-07-27T19:05:19Z","subjects":["biochemistry"],"languages":["eng"],"rights":["Users of works found in University at Buffalo Institutional Repository (UBIR) are responsible for identifying and contacting the copyright owner for permission to reuse. University at Buffalo Libraries do not manage rights for copyright-protected works and cannot assist with permissions.","Copyright retained by author."],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10477/79853","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Richard, John","Chemistry"]},{"key":"dc:creator","label":"Author","values":["He, Rui"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2019-07-30T15:10:30Z","2019","2019-05-10 15:34:56"]},{"key":"dc:publisher","label":"Institution","values":["State University of New York at Buffalo"]},{"key":"dc:type","label":"Dc Type","values":["Text","Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["biochemistry"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Users of works found in University at Buffalo Institutional Repository (UBIR) are responsible for identifying and contacting the copyright owner for permission to reuse. University at Buffalo Libraries do not manage rights for copyright-protected works and cannot assist with permissions.","Copyright retained by author."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/10477/79853"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["M.S.","Three residues function in the activation of glycerol-3-phosphate dehydrogenase from human liver (hlGPDH) for catalysis of reduction of dihydroxyacetone phosphate (DHAP) by NADH: the guanidinium cation of R269 forms a strong ion-pair to the substrate phosphodianion; the amide nitrogen of N270 forms a hydrogen bond to the substrate phosphodianion and lies at one end of a string of hydrogen bonded side chains that bridge the substrate phosphodianion and the carbonyl of DHAP; the amide side chain of Q295 is part of the flexible loop (L292–L297) that closes over the phosphodianion of enzyme-bound DHAP and forms a hydrogen bond to the cationic side chain of R269. Kinetic parameters kcat/Km (M−1 s−1) and kcat/KGAKHPi (M−2 s−1) were determined, respectively, for catalysis of the reduction of DHAP and for dianion activation of reduction of glycolaldehyde (GA) catalyzed by wild-type, Q295G, Q295S, Q295A, and Q295N mutants of hlGPDH.","**To request an accessible version of the file(s) associated with this item, contact library@buffalo.edu. Please include the item's persistent URL [http://hdl.handle.net/. . .] in your request.**"]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Enzyme Architecture: The Role of a Flexible Loop in Activation of Glycerol-3-phosphate Dehydrogenase-Catalyzed Hydride Transfer"]}]}],"canonical_facts":{"dc:contributor":["Richard, John","Chemistry"],"dc:creator":["He, Rui"],"dc:date":["2019-07-30T15:10:30Z","2019","2019-05-10 15:34:56"],"dc:description":["M.S.","Three residues function in the activation of glycerol-3-phosphate dehydrogenase from human liver (hlGPDH) for catalysis of reduction of dihydroxyacetone phosphate (DHAP) by NADH: the guanidinium cation of R269 forms a strong ion-pair to the substrate phosphodianion; the amide nitrogen of N270 forms a hydrogen bond to the substrate phosphodianion and lies at one end of a string of hydrogen bonded side chains that bridge the substrate phosphodianion and the carbonyl of DHAP; the amide side chain of Q295 is part of the flexible loop (L292–L297) that closes over the phosphodianion of enzyme-bound DHAP and forms a hydrogen bond to the cationic side chain of R269. Kinetic parameters kcat/Km (M−1 s−1) and kcat/KGAKHPi (M−2 s−1) were determined, respectively, for catalysis of the reduction of DHAP and for dianion activation of reduction of glycolaldehyde (GA) catalyzed by wild-type, Q295G, Q295S, Q295A, and Q295N mutants of hlGPDH.","**To request an accessible version of the file(s) associated with this item, contact library@buffalo.edu. Please include the item's persistent URL [http://hdl.handle.net/. . .] in your request.**"],"dc:format":["application/pdf"],"dc:identifier":["http://hdl.handle.net/10477/79853"],"dc:language":["eng"],"dc:publisher":["State University of New York at Buffalo"],"dc:rights":["Users of works found in University at Buffalo Institutional Repository (UBIR) are responsible for identifying and contacting the copyright owner for permission to reuse. University at Buffalo Libraries do not manage rights for copyright-protected works and cannot assist with permissions.","Copyright retained by author."],"dc:subject":["biochemistry"],"dc:title":["Enzyme Architecture: The Role of a Flexible Loop in Activation of Glycerol-3-phosphate Dehydrogenase-Catalyzed Hydride Transfer"],"dc:type":["Text","Thesis"]},"updated_at":"2026-07-27T19:05:19Z"}