{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Patti S"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["180"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12343752"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["109(1)"],"pubmed_abstract":["A (S)-selective amine transaminase from a Streptomyces strain, Sbv333-ATA, is a biocatalyst showing both high thermostability with a melting temperature of 85 °C and broad substrate specificity for the amino acceptor. This enzyme was further characterized both biochemically and structurally. The Sbv333-ATA is stable in the presence of up to 20% (v/v) of the water-miscible cosolvents methanol, ethanol, acetonitrile, and dimethyl sulfoxide, and in biphasic systems with petroleum ether, toluene, and ethyl acetate as an organic phase. The enzyme showed also a good activity toward different amino donors, such as (S)-methylbenzylamine and 2-phenylethylamine, aliphatic mono- and di-amines, like propylamine and cadaverine, and selected amino acids. However, more sterically hindered aromatic amines"],"journal":["Applied microbiology and biotechnology"],"pubmed_title":["Functional and structural insights into a thermostable (S)-selective amine transaminase and its improved substrate scope by protein engineering."],"pmcid":["PMC12343752"],"funding_grant_id":["BB/L002035/1"],"pubmed_authors":["Isupov MN","De Rose SA","Magrini Alunno I","Riva S","Patti S","Ferrandi EE","Littlechild JA","Monti D"],"additional_accession":[]},"is_claimable":false,"name":"Functional and structural insights into a thermostable (S)-selective amine transaminase and its improved substrate scope by protein engineering.","description":"A (S)-selective amine transaminase from a Streptomyces strain, Sbv333-ATA, is a biocatalyst showing both high thermostability with a melting temperature of 85 °C and broad substrate specificity for the amino acceptor. This enzyme was further characterized both biochemically and structurally. The Sbv333-ATA is stable in the presence of up to 20% (v/v) of the water-miscible cosolvents methanol, ethanol, acetonitrile, and dimethyl sulfoxide, and in biphasic systems with petroleum ether, toluene, and ethyl acetate as an organic phase. The enzyme showed also a good activity toward different amino donors, such as (S)-methylbenzylamine and 2-phenylethylamine, aliphatic mono- and di-amines, like propylamine and cadaverine, and selected amino acids. However, more sterically hindered aromatic amines","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-06-08T06:51:36.944Z","creation":"2026-06-08T03:14:37.088Z"},"accession":"S-EPMC12343752","cross_references":{"pubmed":["40796981"],"doi":["10.1007/s00253-025-13536-9"]}}