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Reactive Intermediate Deaminase (Rid) protein superfamily includes eight families among which the RidA is conserved in all domains of life. RidA proteins accelerate the deamination of the reactive 2-aminoacrylate (2AA), an enamine produced by some pyridoxal phosphate (PLP)-dependent enzymes. 2AA accumulation inhibits target enzymes with a detrimental impact on fitness. As a consequence of whole genome duplication, teleost fish have two  ridA  paralogs, while other extant vertebrates contain a single-copy gene. We investigated the biochemical properties of the products of two paralogs, identified in  Salmo salar .  Ss RidA-1 and  Ss RidA-2 complemented the growth defect of a  Salmonella enterica ridA  mutant, an  in vivo  model of 2AA stress.  In vitro , both proteins hydrolyzed 2-imino acids (IA) to keto-acids and ammonia.  Ss RidA-1 was active on IA derived from nonpolar amino acids and poorly active or inactive on IA derived from other amino acids tested. In contrast,  Ss RidA-2 had a generally low catalytic efficiency, but showed a relatively higher activity with IA derived from L-Glu and aromatic amino acids. The crystal structures of  Ss RidA-1 and  Ss RidA-2 provided hints of the remarkably different conformational stability and substrate specificity. Overall,  Ss RidA-1 is similar to the mammalian orthologs whereas  Ss RidA-2 displays unique properties likely generated by functional specialization of a duplicated ancestral gene.

Two novel fish paralogs provide insights into the Rid family of imine deaminases active in pre-empting enamine/imine metabolic damage