{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ashley B"],"funding":["Derek Stewart Charitable Trust","Biotechnology and Biological Sciences Research Council"],"pagination":["7997-8002"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10230504"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(21)"],"pubmed_abstract":["We report a chemo-biocatalytic cascade for the synthesis of substituted pyrroles, driven by the action of an irreversible, thermostable, pyridoxal 5'-phosphate (PLP)-dependent, C-C bond-forming biocatalyst (<i>Th</i>AOS). The <i>Th</i>AOS catalyzes the Claisen-like condensation between various amino acids and acyl-CoA substrates to generate a range of α-aminoketones. These products are reacted with β-keto esters in an irreversible Knorr pyrrole reaction. The determination of the 1.6 Å resolution crystal structure of the PLP-bound form of <i>Th</i>AOS lays the foundation for future engineering and directed evolution. This report establishes the AOS family as useful and versatile C-C bond-forming biocatalysts."],"journal":["ACS sustainable chemistry & engineering"],"pubmed_title":["Versatile Chemo-Biocatalytic Cascade Driven by a Thermophilic and Irreversible C-C Bond-Forming α-Oxoamine Synthase."],"pmcid":["PMC10230504"],"funding_grant_id":["BB/J01446X/1","BB/M010996/1","BB/T016841/1","BB/V00168X/1"],"pubmed_authors":["El Ashram A","Basle A","Marles-Wright J","Campopiano DJ","Kelis P","Sajjad M","Ashley B"],"additional_accession":[]},"is_claimable":false,"name":"Versatile Chemo-Biocatalytic Cascade Driven by a Thermophilic and Irreversible C-C Bond-Forming α-Oxoamine Synthase.","description":"We report a chemo-biocatalytic cascade for the synthesis of substituted pyrroles, driven by the action of an irreversible, thermostable, pyridoxal 5'-phosphate (PLP)-dependent, C-C bond-forming biocatalyst (<i>Th</i>AOS). The <i>Th</i>AOS catalyzes the Claisen-like condensation between various amino acids and acyl-CoA substrates to generate a range of α-aminoketones. These products are reacted with β-keto esters in an irreversible Knorr pyrrole reaction. The determination of the 1.6 Å resolution crystal structure of the PLP-bound form of <i>Th</i>AOS lays the foundation for future engineering and directed evolution. This report establishes the AOS family as useful and versatile C-C bond-forming biocatalysts.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 May","modification":"2026-05-29T10:40:03.352Z","creation":"2025-04-19T15:03:08.899Z"},"accession":"S-EPMC10230504","cross_references":{"pubmed":["37266354"],"doi":["10.1021/acssuschemeng.3c00243"]}}