Abstract
Nucleobase deaminases are essential enzymes that are involved in the catabolic pathway and stringently regulate the concentration of the nucleobase derivative pool, which is paramount for nucleotide recycling. This review presents an overview of the structure, function and mechanism of CDA deaminases and their potential as enzyme systems for the development of new antimicrobial therapies. The evolutionary divergence of human nucleobase deaminases with respect to bacterial enzymes has been used as a central theme towards the development of strategies for potential drug targets. Especially, differences in their tertiary fold, active site architectures and mechanisms of regulation have been highlighted in this study. Overall, deaminases present a unique opportunity as drug targets because of their functional plasticity and fidelity.