In vitro inhibition of bovine liver glutamate dehydrogenase by citrinin, a mycotoxin.

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Abstract
Citrinin, a hepato-nephrotoxic antibiotic produced by the fungi Aspergillus and Penicillium which commonly contaminate food, has been shown to increase lipid synthesis in rabbit liver and inhibit cholesterol and triglyceride biosynthesis in rat liver, as well as uncoupling of oxidative phosphorylation [dog heart mitochondria] and decreased oxidation of substrates [rabbit heart mitochondria]. Considering these results, the effects of citrinin on various enzymes (phosphofructokinase EC 2.7.1.56; citrate synthase, EC 4.1.3.7; and glutamate dehydrogenase, EC 1.4.1.3) was studied. Of all the regulatory enzymes tested glutamate dehydrogenase was the only one irreversibly inhibited by citrinin. The possibility of citrinin interaction resulting in depolymerization of the enzyme is implicated but further studies must be done. The other enzymes show competitive inhibition.

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