Role of Two Chloride-Binding Sites in Functioning of Testicular Angiotensin-Converting Enzyme
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- Moiseeva, N.A., Binevski, P.V., Baskin, I.I. et al. Biochemistry (Moscow) (2005) 70: 1167. doi:10.1007/s10541-005-0242-9
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Modeling the structure of the C-domain of bovine angiotensin-converting enzyme revealed two putative chloride-binding sites. The kinetic parameters, Km and kcat, 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.