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Metabolism and Enzymology

Inactivation of 1-Aminocyclopropane-1-Carboxylate Synthase by L-Vinylglycine as Related to the Mechanism-Based Inactivation of the Enzyme by S-Adenosyl-L-Methionine ¹

Department of Biological Sciences, Tohoku University, Kawauchi, Sendai 980, Japan, Mann Laboratory, Department of Vegetable Crops, University of California, Davis, California 95616

The pyridoxal phosphate-dependent 1-aminocyclopropane-1-carboxylate (ACC) synthase catalyzes the conversion of S-adenosyl-L-methionine (AdoMet) to ACC, and is inactivated by AdoMet during the reaction. L-Vinylglycine was found to be a competitive inhibitor of the enzyme, and to cause a time-dependent inactivation of the enzyme. The inactivation required the presence of pyridoxal phosphate and followed pseudo-first-order kinetics at various concentrations of L-vinylglycine. The Michaelis constant for L-vinylglycine in the inactivation reaction (K_inact) was 3.3 millimolar and the maximum rate constant (k_max) was 0.1 per minute. These findings, coupled with the previous observations that the suicidal action of AdoMet involved a covalent linkage of the aminobutyrate portion of AdoMet to the enzyme, support the view that the mechanism-based inactivation of ACC synthase by the substrate AdoMet proceeds through the formation of a vinylglycine-ACC synthase complex as an intermediate.

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