Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase from <i>Desulfomonile tiedjei</i>.

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 Desulfomonile tiedjei, alongside a detailed analysis of PLP binding and holoenzyme stability. This new transaminase exhibits activity toward various D-amino acids and (R)-phenylethylamine. Structural modeling and site-directed mutagenesis of residues in the second shell of the PLP-binding site revealed their roles

SUBMITTER: Bakunova AK 

PROVIDER: S-EPMC12429042 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature