Biochemistry (Moscow)

, Volume 70, Issue 10, pp 1167–1172

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

  • N. A. Moiseeva
  • P. V. Binevski
  • I. I. Baskin
  • V. A. Palyulin
  • O. A. Kost
Article

Abstract

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.

Key words

angiotensin-converting enzyme testicular enzyme C-domain chloride 

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Copyright information

© MAIK "Nauka/Interperiodica" 2005

Authors and Affiliations

  • N. A. Moiseeva
    • 1
  • P. V. Binevski
    • 1
  • I. I. Baskin
    • 1
  • V. A. Palyulin
    • 1
  • O. A. Kost
    • 1
  1. 1.Faculty of ChemistryLomonosov Moscow State UniversityMoscowRussia

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