Effects of the metabolites of the branched-chain amino acids and cysteamine on the glycine cleavage system

Abstract

The effects of ten metabolites of the branched-chain amino acids, CoA and cysteamine (beta-mercaptoethylamine), on the glycine cleavage system were investigated with the liver extracts. It was found that CoA derivatives including tiglyl CoA, isobutyryl CoA, succinyl CoA, methylmalonyl CoA, isovaleryl CoA, propionyl CoA and CoA itself and cysteamine significantly inhibited the glycine cleavage system of the liver extracts. Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.