{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ashley B"],"funding":["RCUK | Biotechnology and Biological Sciences Research Council","Biotechnology and Biological Sciences Research Council"],"pagination":["78"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11906848"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(1)"],"pubmed_abstract":["Carbon-carbon bond formation is one of the key pillars of organic synthesis. Green, selective and efficient biocatalytic methods for such are therefore highly desirable. The α-oxoamine synthases (AOSs) are a class of pyridoxal 5'-phosphate (PLP)-dependent, irreversible, carbon-carbon bond-forming enzymes, which have been limited previously by their narrow substrate specificity and requirement of acyl-CoA thioester substrates. We recently characterized a thermophilic enzyme from Thermus thermophilus (ThAOS) with a much broader substrate scope and described its use in a chemo-biocatalytic cascade process to generate pyrroles in good yields and timescales. Herein, we report the structure-guided engineering of ThAOS to arrive at variants able to use a greatly expanded range of amino acid and s"],"journal":["Communications chemistry"],"pubmed_title":["Rational engineering of a thermostable α-oxoamine synthase biocatalyst expands the substrate scope and synthetic applicability."],"pmcid":["PMC11906848"],"funding_grant_id":["BB/J01446X/1","BB/T016841/1"],"pubmed_authors":["Zhu Y","Basle A","Marles-Wright J","Campopiano DJ","Novikovs N","Sajjad M","Ashley B","Mathew S"],"additional_accession":[]},"is_claimable":false,"name":"Rational engineering of a thermostable α-oxoamine synthase biocatalyst expands the substrate scope and synthetic applicability.","description":"Carbon-carbon bond formation is one of the key pillars of organic synthesis. Green, selective and efficient biocatalytic methods for such are therefore highly desirable. The α-oxoamine synthases (AOSs) are a class of pyridoxal 5'-phosphate (PLP)-dependent, irreversible, carbon-carbon bond-forming enzymes, which have been limited previously by their narrow substrate specificity and requirement of acyl-CoA thioester substrates. We recently characterized a thermophilic enzyme from Thermus thermophilus (ThAOS) with a much broader substrate scope and described its use in a chemo-biocatalytic cascade process to generate pyrroles in good yields and timescales. Herein, we report the structure-guided engineering of ThAOS to arrive at variants able to use a greatly expanded range of amino acid and s","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2026-04-08T19:53:32.315Z","creation":"2026-04-08T14:31:25.857Z"},"accession":"S-EPMC11906848","cross_references":{"pubmed":["40082705"],"doi":["10.1038/s42004-025-01448-8"]}}