Is dUTPase Enzymatic Activity Truly Essential for Viability?

The study of protein enzymatic activities has always been a significant area of scientific and industrial research. The key stages typically undertaken in the characterization of a given enzyme family include establishing the mechanism of catalysis, measuring kinetic parameters, determining structural organization and the architecture of the catalytic center, and subsequential classification. In this review, we address these classical aspects concerning the dUTPase enzyme family, specifically focusing on spatial structure and catalytic activity, while also providing an overview of certain additional functional properties exhibited by some members of this family. The fact of existence of such extra functions raises questions about the reasons for this functional duality. Based on the information known in the literature and our previous research, in this review we conclude that the enzymatic activity of dUTPases suplements other functions independent of the hydrolysis reaction occurring in the catalytic center. In this context, dUTP acts not just as a substrate, but as a signaling molecule, whose binding facilitates the realization of a distinct, non-enzymatic role of dUTPases.