Abstract

The mechanism by which CO2 is formed from glutamate in extracts, of Dictyostelium discoideum does not involve a direct non-oxidative decarboxylation, since the reaction is inhibited anaerobically both in vivo and in vitro. α-Ketoglutarate is implicated as an intermediate in the reaction, since (a) it is decarboxylated at the same rate as glutamate, (b) it competitively dilutes out 14CO2 from [I-14C]glutamate. All the data are compatible with the conclusion that the rate of glutamate oxidation in vivo is substrate-controlled throughout differentiation.

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