Stefano Benini

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: More recent advances are discussed in the comprehension of the specific role of Ni(2+) in the catalysis and the interplay between Ni( 2+) and other metal ions, such as Zn(2-) and Fe(2+), in the metal-dependent enzyme activity.

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: The structure of the complex of urease, a Ni-containing metalloenzyme, with boric acid, supports the proposal that the Ni-bridging hydroxide acts as the nucleophile in the enzymatic process of urea hydrolysis.