ARTICLE: PDF OnlyBünning PeterJournal of Cardiovascular Pharmacology: 1987 - p 31-35 Free Abstract Summary The interaction of angiotensin converting enzyme (ACE) with ramiprilat was studied at pH 7.5 in the presence of 300 mmol/I sodium chloride with furanacryloyl–Phe–Gly–Gly as substrate. Ramiprilat inhibits ACE with a K1 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 ± EI ± 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. Copyright © 1987 Wolters Kluwer Health, Inc. All rights reserved.