<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Patti S</submitter><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>180</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12343752</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>109(1)</volume><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</pubmed_abstract><journal>Applied microbiology and biotechnology</journal><pubmed_title>Functional and structural insights into a thermostable (S)-selective amine transaminase and its improved substrate scope by protein engineering.</pubmed_title><pmcid>PMC12343752</pmcid><funding_grant_id>BB/L002035/1</funding_grant_id><pubmed_authors>Isupov MN</pubmed_authors><pubmed_authors>De Rose SA</pubmed_authors><pubmed_authors>Magrini Alunno I</pubmed_authors><pubmed_authors>Riva S</pubmed_authors><pubmed_authors>Patti S</pubmed_authors><pubmed_authors>Ferrandi EE</pubmed_authors><pubmed_authors>Littlechild JA</pubmed_authors><pubmed_authors>Monti D</pubmed_authors></additional><is_claimable>false</is_claimable><name>Functional and structural insights into a thermostable (S)-selective amine transaminase and its improved substrate scope by protein engineering.</name><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</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Aug</publication><modification>2026-06-08T06:51:36.944Z</modification><creation>2026-06-08T03:14:37.088Z</creation></dates><accession>S-EPMC12343752</accession><cross_references><pubmed>40796981</pubmed><doi>10.1007/s00253-025-13536-9</doi></cross_references></HashMap>