Abstract
1-Aminocyclopropane-1-carboxylate (ACC) synthase, which was partially purified from wounded tomato (Lycoperiscon esculentum Mill.) pericarp tissue, was inactivated by its substrate S-adenosyl-L-methionine (SAM) during its catalytic action. When the partially purified enzyme preparation was incubated with [14C]SAM labeled at different positions and the resulting proteins were analyzed by SDS-PAGE, it was found that ACC synthase was radio-labeled with S-adenosyl-[3,4-14C]methionine and S-adenosyl-[carboxyl-14C]methionine, but not with S-adenosyl-[methyl-14C]methionine. These findings indicated that the 2-aminobutyric acid moiety of SAM molecule was linked covalently into ACC synthase resulting in inactivation of the enzyme.
SAM molecule has two sulfonium diastereomers, (+)− and (−)−SAM (R- and S-configuration at sulfonium center, respectively). When SAM preparations containing different proportions of (+)− and (−)−SAM were used as the substrates, ACC production occurred in proportion to the content of (−)−SAM, whereas the inactivation of the enzyme occurred in proportion to the content of (+)−SAM. These results suggest that (+)−SAM is responsible for the inactivation of ACC synthase.
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© 1989 Kluwer Academic Publishers
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Satoh, S., Yang, S.F. (1989). S-Adenosylmethionine-Dependent Inactivation of 1-Aminocyclopropane-1-Carboxylate Synthase Isolated from Tomato Fruits. In: Clijsters, H., De Proft, M., Marcelle, R., Van Poucke, M. (eds) Biochemical and Physiological Aspects of Ethylene Production in Lower and Higher Plants. Advances in Agricultural Biotechnology, vol 26. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-1271-7_5
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DOI: https://doi.org/10.1007/978-94-009-1271-7_5
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