Kinetic Properties of the Angiotensin Converting Enzyme Inhibitor Ramiprilat
- 1 January 1987
- journal article
- review article
- Published by Wolters Kluwer Health in Journal of Cardiovascular Pharmacology
- Vol. 10, 31-35
- https://doi.org/10.1097/00005344-198706107-00005
Abstract
The interaction of angiotensin converting enzyme (ACE) with ramiprilat was studied at pH 7.5 in the presence of 300 mmol/l sodium chloride with furanacryloyl-Phe-Gly-Gly as substrate. Ramiprilat inhibits ACE with a Ki value of 7 pmol/l. It is both a slow- and tight-binding inhibitor; the mode of inhibition is fully competitive. Binding of ramiprilat to ACE proceeds by a two-step mechanism E + I in equilibrium EI in equilibrium EI* in which the inhibitor rapidly binds to enzyme to form an initial enzyme-inhibitor complex, which then undergoes a slow isomerization. The interaction of ramiprilat with ACE is compared to that of two other potent inhibitors, captopril and enalaprilat.Keywords
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