The inhibition of glutamate dehydrogenase by derivatives of isophthalic acid

Abstract

A range of compounds, structurally related to glutamate, have been tested as inhibitors of pea leaf glutamate dehydrogenase assayed in either direction. Only 5-N-substituted derivatives of aminoisophthalic acid completely inhibited the enzyme when tested at concentrations equal to either those of 2-oxoglutarate or glutamate. A minimum of three carbon atoms attached linearly to the amino group was required for maximum inhibition, inhibition was removed if there was any substitution on the first carbon. The 5-N-substituted derivatives also inhibited yeast (to a greater extent) and bovine liver (to a lesser extent) glutamate dehydrogenases. © 1983.