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Plant and Cell Physiology, 1986, Vol. 27, No. 2 285-291
© 1986

Article

Inactivation of 1-Aminocyclopropane-1-carboxylic Acid Synthase of Etiolated Mung Bean Hypocotyl Segments by its Substrate, S-Adenosyl-L-methionine

Shigeru Satoh and Yohji Esashi

Department of Biological Science, Tohoku University Kawauchi, Sendai 980, Japan

ACC synthase, isolated from mung bean hypocotyl segments treated with IAA and BA, was inactivated by its substrate, SAM, during its catalytic action. The reaction products, ACC and MTA, had no effect on ACC synthase activity. The half-life of the enzyme was 12 min with an initial concentration of 150µM SAM, but this was extended to 23.5 min when the SAM concentration was reduced to 40 µM, near to the endogenous concentration of SAM in mung bean hypocotyl tissue. Addition of AVG, a competitive inhibitor of ACC synthase, to the reaction mixture containing 40 µM SAM, prevented ACC synthase inactivation and increased the half-life about 2-fold. We suggest that ACC synthase inactivation is caused by SAM acting as an enzyme-activated irreversible inactivator (kcat-type inactivator), besides being the substrate for the enzyme. This SAM-dependent inactivation of ACC synthase may explain the rapid inactivation of the enzyme in intact mung bean hypocotyl segments previously found by Yoshii and Imaseki (1982).

(Received October 15, 1985; Accepted December 6, 1985)
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