Inhibition of aconitase by glyoxylate plus oxaloacetate

Abstract

Crude or purified aconitase preparations were inhibited after incubation in the presence of glyoxylate and oxaloacetate. Inhibition was demonstrated with amounts as low as 0.1 ^imole of either glyoxylate or oxaloacetate in the presence of 4 /imoles of oxaloacetate or glyoxylate respectively. Chromatographic evidence is given of the presence of a new compound formed after incubation of the purified enzyme with glyoxylate and oxaloacetate. The presence of the same compound was chromatographically detected after incubation of glyoxylate and oxaloacetate in the presence of Mg, but without enzyme. Spectrophotometric evidence for the disappearance of glyoxylate or oxaloacetate or both is given.