{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bering L"],"funding":["German Research Foundation","GlaxoSmithKline","RCUK | Biotechnology and Biological Sciences Research Council","RCUK | Engineering and Physical Sciences Research Council","Biotechnology and Biological Sciences Research Council","Engineering and Physical Sciences Research Council"],"pagination":["380"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8770729"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["Amides are one of the most fundamental chemical bonds in nature. In addition to proteins and other metabolites, many valuable synthetic products comprise amide bonds. Despite this, there is a need for more sustainable amide synthesis. Herein, we report an integrated next generation multi-catalytic system, merging nitrile hydratase enzymes with a Cu-catalysed N-arylation reaction in a single reaction vessel, for the construction of ubiquitous amide bonds. This synergistic one-pot combination of chemo- and biocatalysis provides an amide bond disconnection to precursors, that are orthogonal to those in classical amide synthesis, obviating the need for protecting groups and delivering amides in a manner unachievable using existing catalytic regimes. Our integrated approach also affords broad s"],"journal":["Nature communications"],"pubmed_title":["Merging enzymes with chemocatalysis for amide bond synthesis."],"pmcid":["PMC8770729"],"funding_grant_id":["EP/V048929/1","BB/R01034X/1","EP/S023755/1"],"pubmed_authors":["Craven EJ","Bering L","Sowerby Thomas SA","Shepherd SA","Micklefield J"],"additional_accession":[]},"is_claimable":false,"name":"Merging enzymes with chemocatalysis for amide bond synthesis.","description":"Amides are one of the most fundamental chemical bonds in nature. In addition to proteins and other metabolites, many valuable synthetic products comprise amide bonds. Despite this, there is a need for more sustainable amide synthesis. Herein, we report an integrated next generation multi-catalytic system, merging nitrile hydratase enzymes with a Cu-catalysed N-arylation reaction in a single reaction vessel, for the construction of ubiquitous amide bonds. This synergistic one-pot combination of chemo- and biocatalysis provides an amide bond disconnection to precursors, that are orthogonal to those in classical amide synthesis, obviating the need for protecting groups and delivering amides in a manner unachievable using existing catalytic regimes. Our integrated approach also affords broad s","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jan","modification":"2026-05-09T03:00:58.79Z","creation":"2025-04-06T14:57:24.857Z"},"accession":"S-EPMC8770729","cross_references":{"pubmed":["35046426"],"doi":["10.1038/s41467-022-28005-4"]}}