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Role of two chloride-binding sites in functioning of testicular angiotensin-converting enzyme.

Authors
Type
Published Article
Journal
Biochemistry. Biokhimii︠a︡
Publication Date
Volume
70
Issue
10
Pages
1167–1172
Identifiers
PMID: 16271036
Source
Medline

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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