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. SsRidA-1 and SsRidA-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. SsRidA-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, SsRidA-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 SsRidA-1 and SsRidA-2 provided hints of the remarkably different conformational stability and substrate specificity. Overall, SsRidA-1 is similar to the mammalian orthologs whereas SsRidA-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 / S. Digiovanni, C. Visentin, G. Degani, A. Barbiroli, M. Chiara, L. Regazzoni, F. Di Pisa, A.J. Brochert, D.M. Downs, S. Ricagno, M.A. Vanoni, L. Popolo. - In: SCIENTIFIC REPORTS. - ISSN 2045-2322. - 10:1(2020 Jun 23), pp. 10135.1-10135.14.
Titolo: | Two Novel Fish Paralogs Provide Insights Into the Rid Family of Imine Deaminases Active in Pre-Empting enamine/imine Metabolic Damage |
Autori: | |
Parole Chiave: | Metabolic damage; Reactive intermediate deaminases; Salmon salar; gene duplication; Protein stability; telost fish; PLP-dependent enzymes |
Settore Scientifico Disciplinare: | Settore BIO/10 - Biochimica Settore BIO/11 - Biologia Molecolare Settore CHIM/08 - Chimica Farmaceutica |
Data di pubblicazione: | 23-giu-2020 |
Rivista: | |
Tipologia: | Article (author) |
Data ahead of print / Data di stampa: | 23-gen-2020 |
Digital Object Identifier (DOI): | http://dx.doi.org/10.1038/s41598-020-66663-w |
Appare nelle tipologie: | 01 - Articolo su periodico |
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