Kinetic properties of the angiotensin converting enzyme inhibitor ramiprilat.

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.

journal_name

J Cardiovasc Pharmacol

authors

Bünning P

doi

10.1097/00005344-198706107-00005

subject

Has Abstract

pub_date

1987-01-01 00:00:00

pages

S31-5

eissn

0160-2446

issn

1533-4023

journal_volume

10 Suppl 7

pub_type

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