Some properties of guinea pig brain glutamate decarboxylase and its inhibition by the convulsant allylglycine (2-amino-4-pentenoic acid)

—Glutamate decarboxylase (l -glutamate 1-carboxy-lyase EC 4.1.1.15; GAD) has been isolated from guinea pig brain and some of its properties studied. Many of its properties indicated that it was similar if not identical to the decarboxylase isolated from other species. It showed normal Michaelis-Menten kinetics (K_m= 8 mM), had a pH optimum of 6.6–7.0 and was protected by sulphydryl reagents. Its activity was stimulated by pyridoxal phosphate and inhibited by a variety of anions, cations and carbonyl trapping agents. Allylglycine strongly inhibited GAD isolated from the brains of several different species. The mechanism of this inhibition has been studied kinetically and compared to chloride induced inhibition. The kinetic data presented is consistent with the idea that allylglycine inhibits the enzyme by a partially reversible inactivation rather than by reversible competitive inhibition.