Silvia Miletti

TL;DR: The mode of binding of the inhibitor, and a comparison between the native and inhibited urease structures, indicate a novel mechanism for enzymatic urea hydrolysis which reconciles the available structural and biochemical data.

TL;DR: In this article, a comprehensive critical summary of urease spectroscopy, crystallography, inhibitor binding, and site-directed mutagenesis, with special emphasis given to the relationships between the structural features of the Ni-containing active site and the physico-chemical and biochemical properties of this metallo-enzyme.

TL;DR: The structure of Bacillus pasteurii urease inhibited with acetohydroxamic acid was solved and refined anisotropically using synchrotron X-ray cryogenic diffraction data to show the binding mode of the inhibitor anion and the possible implications of the results on structure-based molecular design of new Urease inhibitors are discussed.

TL;DR: Jack bean urease was adsorbed and immobilized on hydroxyapatite, a stable calcium phosphate mineral commonly found in alkaline soils and its stability and kinetic properties were investigated to derive a model that explains the stabilisation of Urease in alkali soil.

TL;DR: BpUreE has a high sequence similarity with UreE proteins isolated from different biological sources, while no sequence homology is observed with proteins belonging to different classes.