Amine transaminases (ATAs) are used to synthesize enantiomerically pure amines, which are building blocks for pharmaceuticals and agrochemicals.
R-selective ATAs belong to the fold type IV PLP-dependent enzymes, and different sequence-, structure- and substrate scope-based features have been identified in the past decade. However, our knowledge is still restricted due to the limited number of characterized (
R)-ATAs, with additional bias towards fungal origin. We aimed to expand the toolbox of (
R)-ATAs and contribute to the understanding of this enzyme subfamily. We identified and characterized four new (
R)-ATAs. The ATA from
Exophiala sideris contains a motif characteristic for d -ATAs, which was previously believed to be a disqualifying factor for (
R)-ATA activity. The crystal structure of the ATA from
Shinella is the first from a Gram-negative bacterium. The ATAs from
Pseudonocardia acaciae and
Tetrasphaera japonica are the first characterized (
R)-ATAs with a shortened/missing N-terminal helix. The active-site charges vary significantly between the new and known ATAs, correlating with their diverging substrate scope.
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