Revisiting the Non-Animal Peroxidase Superfamily

Peroxidases reduce peroxide through substrate oxidation in order to alleviate oxidative stress in aerobic organisms. Since the initial description of the non-animal peroxidase superfamily, great effort has been made to characterize this large and heterogeneous group of proteins. Next generation sequencing data have permitted an in-depth study of the molecular evolution of this superfamily and allowed us to perform a phylogenetic reconstruction. Through this analysis, we identified two additional class I members and, here, we discuss the similarities and differences among members of this class. Our results provide new insights into the organization of these antioxidant enzymes, allowing us to propose a new model for the emergence and evolution of this superfamily.

TrendsThe non-animal peroxidases superfamily was first described in 1992 and named plant, fungal, and bacterial peroxidases superfamily. Since then, the identification of members in other groups of organisms has motivated the first name change and opinions are currently divided regarding the need for further name updates.In the past few years, phylogenetic analyses performed from increasingly larger datasets have suggested that some superfamily groups should be further subdivided and reorganized inside the superfamily classes; however, most results were not well supported and, therefore, are largely inconclusive.Apart from their scavenging activity, these proteins act as regulators of the hydrogen peroxide signaling. An accurate classification of each member should provide insights for functional studies aiming to understand the role these enzymes play in plant defense and development.