{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/85468"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/85468","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Enzymes as Drug Targets in the Isoprenoid Biosynthesis Pathway: Structure, Mechanism and Inhibition","abstract":"Enzymes in isoprenoid biosynthesis pathway play important roles in all living organisms. Several of them have been identified as drug targets. Here we reported the inhibition study of isopentenyl diphosphate/dimethylallyl diphosphate isomerase (IPPI) and deoxyzylolus reductoisomerase (DXR), along with crystal structures of enzyme inhibitor complexes. A high throughput screening method was developed, by which novel potent inhibitors against farnesyl diphosphate synthase (FPPS) and Staph. Aureus dehydrosqulene synthase (CrtM) were identified. We also conducted thermodynamic study of FPPS inhibition, which revealed that both enthalpy and antropy driven binding inhibitors have similar activity.","abstract_html":"Enzymes in isoprenoid biosynthesis pathway play important roles in all living organisms. Several of them have been identified as drug targets. Here we reported the inhibition study of isopentenyl diphosphate/dimethylallyl diphosphate isomerase (IPPI) and deoxyzylolus reductoisomerase (DXR), along with crystal structures of enzyme inhibitor complexes. A high throughput screening method was developed, by which novel potent inhibitors against farnesyl diphosphate synthase (FPPS) and Staph. Aureus dehydrosqulene synthase (CrtM) were identified. We also conducted thermodynamic study of FPPS inhibition, which revealed that both enthalpy and antropy driven binding inhibitors have similar activity.","abstract_has_math":false,"creators":["Yin, Fenglin"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biophysics and Computational Biology","degree_department":null,"school":null,"contributors":["Oldfield, Eric"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:46:11Z","date_published":"2015-09-25T22:46:11Z","updated_at":"2026-07-22T22:26:25Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3314948"],"render_values":[{"text":"(MiAaPQ)AAI3314948","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/85468","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Oldfield, Eric"]},{"key":"dc:creator","label":"Author","values":["Yin, Fenglin"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:46:11Z","10000-01-01","2008"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biophysics and Computational Biology"]},{"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/2142/85468","(MiAaPQ)AAI3314948"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Enzymes in isoprenoid biosynthesis pathway play important roles in all living organisms. Several of them have been identified as drug targets. Here we reported the inhibition study of isopentenyl diphosphate/dimethylallyl diphosphate isomerase (IPPI) and deoxyzylolus reductoisomerase (DXR), along with crystal structures of enzyme inhibitor complexes. A high throughput screening method was developed, by which novel potent inhibitors against farnesyl diphosphate synthase (FPPS) and Staph. Aureus dehydrosqulene synthase (CrtM) were identified. We also conducted thermodynamic study of FPPS inhibition, which revealed that both enthalpy and antropy driven binding inhibitors have similar activity.","Made available in DSpace on 2015-09-25T22:46:11Z (GMT). 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Here we reported the inhibition study of isopentenyl diphosphate/dimethylallyl diphosphate isomerase (IPPI) and deoxyzylolus reductoisomerase (DXR), along with crystal structures of enzyme inhibitor complexes. A high throughput screening method was developed, by which novel potent inhibitors against farnesyl diphosphate synthase (FPPS) and Staph. Aureus dehydrosqulene synthase (CrtM) were identified. We also conducted thermodynamic study of FPPS inhibition, which revealed that both enthalpy and antropy driven binding inhibitors have similar activity.","Made available in DSpace on 2015-09-25T22:46:11Z (GMT). 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