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Role of two chloride-binding sites in functioning of testicular angiotensin-converting enzyme
N A Moiseeva1, P V Binevski, I I Baskin
1Faculty of Chemistry, Lomonosov Moscow State University, Moscow, 119992, Russia. znatali@enzyme.chem.msu.ru
Abstract:
Modeling the structure of the C-domain of bovine angiotensin-converting enzyme revealed two putative chloride-binding sites. The kinetic parameters, K(m) and k(cat), of hydrolysis of the substrate Cbz-Phe-His-Leu catalyzed by the testicular (C-domain) enzyme were determined over a wide range of chloride concentrations. Chloride anions were found to be enzyme activators at relatively low concentrations, but they inhibit enzymatic activity at high concentrations. A general scheme for the effect of chloride anions on activity of the C-domain of bovine angiotensin-converting enzyme accounting for binding the "activating" and "inhibiting" anions is suggested.
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