Abstract
Abstract
The nucleotide ATP was shown to be a reversible inhibitor of partially purified γ-aminobutyrate aminotransferase isolated from mouse brain. This inhibition was of the competitive type with respect to the substrate, γ-aminobutyric acid (K i = 3.7 ± 0.6 mM), but was noncompetitive with respect to both the second substrate α-ketoglutarate and the cofactor pyridoxal 5′-phosphate. Two analogues of ATP, ADP and GTP, also gave rise to an inhibition γ-aminobutyrate aminotransferase that was similar to that produced by ATP. These results are consistent with the view that mouse brain γ-aminobutyric acid aminotransferase could be under regulatory control by ATP and certain other nucleotides within the mitochondria.
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