{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(14)"],"submitter":["Karvelis E"],"pubmed_abstract":["The task of adapting enzymes for specific applications is often hampered by our incomplete ability to tune and tailor catalytic functions, particularly when seeking increased activity. Here, we develop and demonstrate a rational approach to address this challenge, applied to ketol-acid reductoisomerase (KARI), which has uses in industrial-scale isobutanol production. While traditional structure-based computational enzyme redesign strategies typically focus on the enzyme-bound ground state (GS) and transition state (TS), we postulated that additionally treating the underlying dynamics of complete turnover events that connect and pass through both states could further elucidate the structural properties affecting catalysis and help identify mutations that lead to increased catalytic activity"],"journal":["ACS catalysis"],"pagination":["10491-10509"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11264209"],"repository":["biostudies-literature"],"pubmed_title":["Substrate Turnover Dynamics Guide Ketol-Acid Reductoisomerase Redesign for Increased Specific Activity."],"pmcid":["PMC11264209"],"pubmed_authors":["Swanson C","Karvelis E","Tidor B"],"additional_accession":[]},"is_claimable":false,"name":"Substrate Turnover Dynamics Guide Ketol-Acid Reductoisomerase Redesign for Increased Specific Activity.","description":"The task of adapting enzymes for specific applications is often hampered by our incomplete ability to tune and tailor catalytic functions, particularly when seeking increased activity. Here, we develop and demonstrate a rational approach to address this challenge, applied to ketol-acid reductoisomerase (KARI), which has uses in industrial-scale isobutanol production. While traditional structure-based computational enzyme redesign strategies typically focus on the enzyme-bound ground state (GS) and transition state (TS), we postulated that additionally treating the underlying dynamics of complete turnover events that connect and pass through both states could further elucidate the structural properties affecting catalysis and help identify mutations that lead to increased catalytic activity","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-01T20:31:10.898Z","creation":"2025-05-18T13:26:32.611Z"},"accession":"S-EPMC11264209","cross_references":{"pubmed":["39050899"],"doi":["10.1021/acscatal.4c01446"]}}