A molecular modeling study of the urease active site

Urease catalyzes the decomposition of urea to ammonium and carbamate ions by its active site which contains two nickel(II) atoms. Here we report the results of a molecular dynamics investigation performed on a system constituted of the cavity of the enzyme and one hydroxamic acid molecule which acts as an inhibitor of the protein. The results agree with experimental data and represent a valid starting point for the design of more efficient urease inhibitors. (C) 1997 Elsevier Science B.V.