THE INHIBITION OF GLUTAMATE DEHYDROGENASE BY DERIVATIVES OF ISOPHTHALIC ACID

Article abstract of DOI:10.1016/S0031-9422(00)84014-5

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.Key Word Index - Pisum sativum; Leguminoseae; yeast; bovine; glutamate dehydrogenase inhibition; isophthalic acid derivatives.