Structural landscape of bacterial urease: implications for catalyst and adaptation

Bacterial ureases are unique enzymes full of paradoxes. They catalyze a simple hydrolysis reaction yet embody an architectural marvel of quaternary organization, comprising multiple subunits and requiring complex accessory systems for maturation. This review scrutinizes ureases from a structural perspective, exploring the diversity of their oligomeric assemblies in pathogenic and soil bacteria, the detailed coordination chemistry of the nickel-containing active site, and the conformational dynamics of other catalytic elements. Furthermore, it explains the structural changes that occur in response to environmental factors, including pH, temperature, and inhibitors. The analysis also encompasses genetic regulation and the design of expression systems for biotechnological applications. Knowledge of urease structural biology will guide future efforts to redesign this enzyme for specific purposes across diverse scientific contexts.