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;
1997-01-01
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
