{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bakunova AK"],"funding":["The Ministry of Science and Higher Education of the Russian Federation","The Russian Science Foundation"],"pagination":["8536"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12429042"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(17)"],"pubmed_abstract":["Understanding the structure-function relationships of pyridoxal-5'-phosphate (PLP)-dependent transaminases is key to advancing pyridoxal-phosphate-dependent catalysis and engineering transaminases for industrial applications. Despite our extensive knowledge of PLP-dependent enzymatic reactions, engineering transaminase activity and stability remains challenging. Here, we present the functional characterization of a novel PLP-dependent fold type IV transaminase from <i>Desulfomonile tiedjei</i>, alongside a detailed analysis of PLP binding and holoenzyme stability. This new transaminase exhibits activity toward various D-amino acids and (<i>R</i>)-phenylethylamine. Structural modeling and site-directed mutagenesis of residues in the second shell of the PLP-binding site revealed their roles "],"journal":["International journal of molecular sciences"],"pubmed_title":["Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase from &lt;i&gt;Desulfomonile tiedjei&lt;/i&gt;."],"pmcid":["PMC12429042"],"funding_grant_id":["23-74-30004"],"pubmed_authors":["Popov VO","Bakunova AK","Bezsudnova EY","Rudina IV"],"additional_accession":[]},"is_claimable":false,"name":"Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase from &lt;i&gt;Desulfomonile tiedjei&lt;/i&gt;.","description":"Understanding the structure-function relationships of pyridoxal-5'-phosphate (PLP)-dependent transaminases is key to advancing pyridoxal-phosphate-dependent catalysis and engineering transaminases for industrial applications. Despite our extensive knowledge of PLP-dependent enzymatic reactions, engineering transaminase activity and stability remains challenging. Here, we present the functional characterization of a novel PLP-dependent fold type IV transaminase from <i>Desulfomonile tiedjei</i>, alongside a detailed analysis of PLP binding and holoenzyme stability. This new transaminase exhibits activity toward various D-amino acids and (<i>R</i>)-phenylethylamine. Structural modeling and site-directed mutagenesis of residues in the second shell of the PLP-binding site revealed their roles ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-04-08T19:37:28.694Z","creation":"2026-04-08T13:55:54.902Z"},"accession":"S-EPMC12429042","cross_references":{"pubmed":["40943456"],"doi":["10.3390/ijms26178536"]}}