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

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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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Authors and Affiliations

  1. Faculty of Chemistry, Lomonosov Moscow State University, 119992, Moscow, Russia

    N. A. Moiseeva, P. V. Binevski, I. I. Baskin, V. A. Palyulin & O. A. Kost

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  1. N. A. Moiseeva
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  2. P. V. Binevski
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  3. I. I. Baskin
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  4. V. A. Palyulin
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  5. O. A. Kost
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Correspondence to N. A. Moiseeva.

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__________

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.

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Moiseeva, N.A., Binevski, P.V., Baskin, I.I. et al. Role of Two Chloride-Binding Sites in Functioning of Testicular Angiotensin-Converting Enzyme. Biochemistry (Moscow) 70, 1167–1172 (2005). https://doi.org/10.1007/s10541-005-0242-9

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  • DOI: https://doi.org/10.1007/s10541-005-0242-9

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