Mode of action and characteristics of monoamine oxidase-A inhibition by moclobemide

The mode of interaction of the reversible monoamine oxidase-A (MAO-A) inhibitor moclobemide with the enzyme was investigated. The inhibition of rat brain or human placenta MAO-A by moclobemide showed an initial competitive phase, with a relatively low affinity (KI = 0.2-0.4 mM). However, the potency...

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Bibliographic Details
Published in:Psychopharmacologia 1992-02, Vol.106 (S1), p.S15-S16
Main Authors: CESURA, A. M, KETTLER, R, IMHOF, R, DA PRADA, M
Format: Article
Language:English
Subjects:
Atomic and molecular physics
Atomic properties and interactions with photons
Benzamides - pharmacology
Binding Sites - drug effects
Brain - drug effects
Brain - enzymology
Exact sciences and technology
Female
Humans
Kinetics
Mitochondria - drug effects
Mitochondria - enzymology
Moclobemide
Monoamine Oxidase - metabolism
Monoamine Oxidase Inhibitors - pharmacology
Physics
Placenta - enzymology
Pregnancy
Tyramine - metabolism
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Summary:The mode of interaction of the reversible monoamine oxidase-A (MAO-A) inhibitor moclobemide with the enzyme was investigated. The inhibition of rat brain or human placenta MAO-A by moclobemide showed an initial competitive phase, with a relatively low affinity (KI = 0.2-0.4 mM). However, the potency of the inhibitor was increased with incubation time. The time-dependent component of the association of moclobemide with MAO-A followed pseudo-first order kinetics. In contrast to mechanism-based inhibitors, no indication for adduct or product formation was detected after incubation of moclobemide with the enzyme. Even though some aspects of the moclobemide interaction with MAO-A are still not completely elucidated, this compound seems to have the characteristics of a slow-binding inhibitor.
ISSN:0033-3158
1432-2072
DOI:10.1007/BF02246226