{"id":{"repo_id":"twu","oai_identifier":"oai:twu-ir.tdl.org:11274/11084"},"canonical_url":"https://search.dev.ndltd.org/etd/twu/oai:twu-ir.tdl.org:11274/11084","repository":{"repo_id":"twu","name":"Texas Woman's University","base_url":"https://twu-ir.tdl.org/server/oai/request"},"display":{"title":"Glutathione synthetase: Conserved residues of the substrate loop","abstract":"The important antioxidant tripeptide glutathione (GSH) is synthesized in two ATP-dependent steps; the second enzyme in the biosynthetic pathway, glutathione synthetase (GS), ligates glycine to γ-glutamylcysteine (γ-GC). Human glutathione synthetase (hGS) deficiency causes hemolytic anemia, metabolic acidosis, 5-oxprolinuria and a total deficiency may be lethal. Three flexible loops (A, G and S) surround the substrates (ATP, glycine and γ-GC). Human glutathione synthetase is negatively cooperative to one substrate, γ-GC. The Substrate- or S-loop is proximal to γ-GC and thought to participate in γ-GC binding. The S-loop (266-FRDGYMPRQYS-276) contains 11 residues, some of which are highly conserved (F266, R267, G269, Y270, P272 and Y275). Site directed mutagenesis was used to change these highly conserved S-loop residues, and then their roles in substrate binding, enzyme activity and stability were assessed.","abstract_html":"The important antioxidant tripeptide glutathione (GSH) is synthesized in two ATP-dependent steps; the second enzyme in the biosynthetic pathway, glutathione synthetase (GS), ligates glycine to γ-glutamylcysteine (γ-GC). Human glutathione synthetase (hGS) deficiency causes hemolytic anemia, metabolic acidosis, 5-oxprolinuria and a total deficiency may be lethal. Three flexible loops (A, G and S) surround the substrates (ATP, glycine and γ-GC). Human glutathione synthetase is negatively cooperative to one substrate, γ-GC. The Substrate- or S-loop is proximal to γ-GC and thought to participate in γ-GC binding. The S-loop (266-FRDGYMPRQYS-276) contains 11 residues, some of which are highly conserved (F266, R267, G269, Y270, P272 and Y275). Site directed mutagenesis was used to change these highly conserved S-loop residues, and then their roles in substrate binding, enzyme activity and stability were assessed.","abstract_has_math":false,"creators":["Shrestha, Bisesh"],"institution":"Texas Woman's University","degree_name":"Master of Science","degree_level":"Master","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":["Anderson, Mary"],"committee_members":["Britt, Mark","Anderson, Mary E.","Sheardy, Richard Dean"],"year":2013,"date_issued":"2013-05","date_published":"2013-05","updated_at":"2026-07-24T05:05:11Z","subjects":["Pure sciences","Biological sciences","Active site","Anion-pi","Arginine","Cooperativity","Glutathione synthetase","Tryptophan"],"languages":["en_US"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/11274/11084","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeechair","label":"Committee Chair","values":["Anderson, Mary"]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Britt, Mark","Anderson, Mary E.","Sheardy, Richard Dean"]},{"key":"dc:creator","label":"Author","values":["Shrestha, Bisesh"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2019-03-07T16:45:23Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2019-03-07T16:45:23Z"]},{"key":"dc:date.issued","label":"Date","values":["2013-05"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Master"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Texas Woman's University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Pure sciences","Biological sciences","Active site","Anion-pi","Arginine","Cooperativity","Glutathione synthetase","Tryptophan"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en_US"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/11274/11084"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The important antioxidant tripeptide glutathione (GSH) is synthesized in two ATP-dependent steps; the second enzyme in the biosynthetic pathway, glutathione synthetase (GS), ligates glycine to γ-glutamylcysteine (γ-GC). Human glutathione synthetase (hGS) deficiency causes hemolytic anemia, metabolic acidosis, 5-oxprolinuria and a total deficiency may be lethal. Three flexible loops (A, G and S) surround the substrates (ATP, glycine and γ-GC). Human glutathione synthetase is negatively cooperative to one substrate, γ-GC. The Substrate- or S-loop is proximal to γ-GC and thought to participate in γ-GC binding. The S-loop (266-FRDGYMPRQYS-276) contains 11 residues, some of which are highly conserved (F266, R267, G269, Y270, P272 and Y275). Site directed mutagenesis was used to change these highly conserved S-loop residues, and then their roles in substrate binding, enzyme activity and stability were assessed."]},{"key":"dc:title","label":"Title","values":["Glutathione synthetase: Conserved residues of the substrate loop"]}]}],"canonical_facts":{"dc:contributor.committeechair":["Anderson, Mary"],"dc:contributor.committeemember":["Britt, Mark","Anderson, Mary E.","Sheardy, Richard Dean"],"dc:creator":["Shrestha, Bisesh"],"dc:date.accessioned":["2019-03-07T16:45:23Z"],"dc:date.available":["2019-03-07T16:45:23Z"],"dc:date.issued":["2013-05"],"dc:description.abstract":["The important antioxidant tripeptide glutathione (GSH) is synthesized in two ATP-dependent steps; the second enzyme in the biosynthetic pathway, glutathione synthetase (GS), ligates glycine to γ-glutamylcysteine (γ-GC). Human glutathione synthetase (hGS) deficiency causes hemolytic anemia, metabolic acidosis, 5-oxprolinuria and a total deficiency may be lethal. Three flexible loops (A, G and S) surround the substrates (ATP, glycine and γ-GC). Human glutathione synthetase is negatively cooperative to one substrate, γ-GC. The Substrate- or S-loop is proximal to γ-GC and thought to participate in γ-GC binding. The S-loop (266-FRDGYMPRQYS-276) contains 11 residues, some of which are highly conserved (F266, R267, G269, Y270, P272 and Y275). Site directed mutagenesis was used to change these highly conserved S-loop residues, and then their roles in substrate binding, enzyme activity and stability were assessed."],"dc:identifier.uri":["https://hdl.handle.net/11274/11084"],"dc:language.iso":["en_US"],"dc:subject":["Pure sciences","Biological sciences","Active site","Anion-pi","Arginine","Cooperativity","Glutathione synthetase","Tryptophan"],"dc:title":["Glutathione synthetase: Conserved residues of the substrate loop"],"dc:type":["Thesis"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Master"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Texas Woman's University"]},"updated_at":"2026-07-24T05:05:11Z"}