{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liao J"],"funding":["Deutsche Forschungsgemeinschaft","Deutsche Forschungsgemeinschaft (German Research Foundation)","King Abdullah University of Science and Technology"],"pagination":["3065"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11954892"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["Enzymes are essential catalysts in biological systems. Substrate inhibition, once dismissed, is now observed in 20% of enzymes<sup>1</sup> and is attributed to the formation of an unproductive enzyme-substrate complex, with no structural evidence of unproductivity provided to date<sup>1-6</sup>. This study uncovers the molecular mechanism of substrate inhibition in tobacco glucosyltransferase NbUGT72AY1, which transfers glucose to phenols for plant protection. The peculiarity that β-carotene strongly attenuates the substrate inhibition of NbUGT72AY1, despite being a competitive inhibitor, allows to determine the conformational changes that occur during substrate binding in both active and substrate-inhibited complexes. Crystallography reveals structurally different ternary enzyme-substrate"],"journal":["Nature communications"],"pubmed_title":["β-Carotene alleviates substrate inhibition caused by asymmetric cooperativity."],"pmcid":["PMC11954892"],"funding_grant_id":["SCHW 634/34-1"],"pubmed_authors":["Steinchen W","Hoffmann TD","Kurze E","Song C","Di Pizio A","Nicoli A","Catici DAM","Kuttler C","Shahul Hameed UF","Liao J","Schwab WG","Assaad-Gerbert F","Arold ST","Sun G","Hoffmann T"],"additional_accession":[]},"is_claimable":false,"name":"β-Carotene alleviates substrate inhibition caused by asymmetric cooperativity.","description":"Enzymes are essential catalysts in biological systems. Substrate inhibition, once dismissed, is now observed in 20% of enzymes<sup>1</sup> and is attributed to the formation of an unproductive enzyme-substrate complex, with no structural evidence of unproductivity provided to date<sup>1-6</sup>. This study uncovers the molecular mechanism of substrate inhibition in tobacco glucosyltransferase NbUGT72AY1, which transfers glucose to phenols for plant protection. The peculiarity that β-carotene strongly attenuates the substrate inhibition of NbUGT72AY1, despite being a competitive inhibitor, allows to determine the conformational changes that occur during substrate binding in both active and substrate-inhibited complexes. Crystallography reveals structurally different ternary enzyme-substrate","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2026-06-01T19:09:25.814Z","creation":"2025-06-25T03:04:33.883Z"},"accession":"S-EPMC11954892","cross_references":{"pubmed":["40157902"],"doi":["10.1038/s41467-025-58259-7"]}}