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. 1983 Feb 15;221(1):143-7.
doi: 10.1016/0003-9861(83)90130-3.

Kinetic mechanism of bovine liver argininosuccinate lyase

F M Raushel, R Nygaard

Kinetic mechanism of bovine liver argininosuccinate lyase

F M Raushel et al. Arch Biochem Biophys. .

Abstract

The kinetic mechanism of bovine liver argininosuccinate lyase has been determined at pH 7.5, 25 degrees C. Fumarate and arginine are both noncompetitive inhibitors versus argininosuccinate. The dead-end inhibitor, succinate, is competitive versus fumarate and argininosuccinate, but noncompetitive versus arginine. Citrulline is competitive versus arginine and noncompetitive versus argininosuccinate and fumarate. The results are consistent with a random mechanism with the formation of two dead-end complexes: E . argininosuccinate . fumarate and E . argininosuccinate . arginine. No evidence was obtained for nonlinear reciprocal plots. The equilibrium constant was found to be 3.7 mM.

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