, Volume 70, Issue 10, pp 1167-1172

Role of Two Chloride-Binding Sites in Functioning of Testicular Angiotensin-Converting Enzyme

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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, 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.

Translated from Biokhimiya, Vol. 70, No. 10, 2005, pp. 1415–1422.
Original Russian Text Copyright © 2005 by Moiseeva, Binevski, Baskin, Palyulin, Kost.
Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM04-392, May 23, 2005.