Nov 1, 1975

The action of chelating agents on human liver aldehyde dehydrogenase

The Biochemical Journal
R S Sidhu, A H Blair

Abstract

Human liver aldehyde dehydrogenase was inhibited by aromatic chelating agents. However, structurally related compounds with much lower metal-complexing ability displayed affinities for enzyme essentially equal to those of their respective chelating analogues. Inhibition was competitive with respect to the coenzyme. It is suggested that hydrophobic interactions between the inhibitors and the coenzyme-binding site of the enzyme are responsible for the observed effects on activity.

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Mentioned in this Paper

Bipyridyl
Aldehyde Oxidoreductases
Metal Antagonists
Liver
ALDH3A1
Phenanthrolines
Coenzymes

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