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- W2000873137 abstract "1. The effect of different inorganic anions on the catalytic activity of native and subunit aspartate transcarbamylase (carbamoylphosphate: l-aspartate carbamoltransferase, EC 2.1.3.2) has been investigated at pH 7.0 and 25°. 2. Several inorganic anions were found to inhibit both native and subunit aspartate transcarbamylase. The order of effectiveness for the best inhibitors was: PPi > F− > Pi > SO42−. 3. For each ion except F−, a strict competitive relationship was observed between the anion inhibitors and the substrate carbamyl phosphate. 4. The concentration of l-aspartate also greatly influenced the magnitude of the inhibition. The inhibition increased with increasing concentration of l-aspartate. 5. The effect of F− was shown to be due to a displacement of the pH curve along the pH axis. F− inhibited native asparatate transcarbamylase below pH 8 and activated it above this pH. 6. Possible mechanisms of inhibition are discussed, and it is suggested that an inhibitor-l-aspartate complex is formed at the active site." @default.
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- W2000873137 date "1966-09-01" @default.
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- W2000873137 title "Aspartate transcarbamylase from Escherichia coli I. Inhibition by inorganic anions" @default.
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- W2000873137 doi "https://doi.org/10.1016/0926-6593(66)90037-3" @default.
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