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.

A molecular modeling study of the urease active site / Manunza, Bruno Mario Luigi; Deiana, Salvatore Andrea; Pintore, M; Solinas, V; Gessa, C.. - In: JOURNAL OF MOLECULAR STRUCTURE. THEOCHEM. - ISSN 0166-1280. - 419:1(1997), pp. 33-36.

A molecular modeling study of the urease active site

MANUNZA, Bruno Mario Luigi;DEIANA, Salvatore Andrea;
1997

Abstract

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.
A molecular modeling study of the urease active site / Manunza, Bruno Mario Luigi; Deiana, Salvatore Andrea; Pintore, M; Solinas, V; Gessa, C.. - In: JOURNAL OF MOLECULAR STRUCTURE. THEOCHEM. - ISSN 0166-1280. - 419:1(1997), pp. 33-36.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11388/47212
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