Inhibition of Glutamate Dehydrogenase by 2-Oxoglutarate (OGA) in Klebsiella aerogenes 19-35, a Glutamate-Producing Bacterium

Abstract

The enzymatic properties of partially purified glutamate dehydrogenase (GDH) from K. aerogenes 19-35 were investigated. It was found that GDH, responsible for reductive amination, was subject to substrate inhibition and product inhibition. The substrate inhibition was specific for OGA. In oxidative deamination, no substrate inhibition was observed, although product inhibition occurred. The enzyme was inhibited by malate, fumarate and succinate in biosynthetic reaction, although these organic acids stimulated the activity of GDH in degradative reaction.