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Plant and Cell Physiology, 1997, Vol. 38, No. 3 312-318
© 1997

Inhibition by 1-Aminocyclobutane-l-Carboxylate of the Activity of 1-Aminocyclopropane-l-Carboxylate Oxidase Obtained from Senescing Petals of Carnation {Dianthus caryophyllus L.) Flowers

Yusuke Kosugi1, Naoko Oyamada1,2, Shigeru Satoh1,3, Toshihito Yoshioka1, Ei-ichi Onodera2 and Yuko Yamada2

1 Laboratory of Bio-adaptation, Graduate School of Agriculture, Tohoku University Tsutsumidori-amamiyamachi 1-1, Aoba-ku, Sendai, 981 Japan
2 Miyagi Horticultural Experimental Station Natori, Miyagi, 982-12 Japan

3To whom inquiries should be addressed: fax, +81/0-22-717-8834; e-mail, ssatoh{at}bios.tohoku.ac.jp

We partially purified 1-aminocyclopropane-l-carboxy-late (ACC) oxidase from senescing petals of carnation {Dianthus caryophyllus L. cv. Nora) flowers and investigated its general characteristics, and, in particular, the inhibition of its activity by ACC analogs. The enzyme had an optimum pH at 7-7.5 and required Fe2+, ascorbate and NaHCO3 for its maximal activity. The Km for ACC was calculated as 111-125 µM in the presence of NaHCO3. Its Mr was estimated to be 35 and 36 kDa by gel-filtration chromatography on HPLC and SDS-PAGE, respectively, indicating that the enzyme exists in a monomeric form. These properties were in agreement with those reported previously with ACC oxidases from different plant tissues including senescing carnation petals. Among six ACC analogs tested, l-aminocyclobutane-l-carboxylate (ACBC) inhibited most severely the activity of ACC oxidase from carnation petals. ACBC acted as a competitive inhibitor with the Ki of 20-31 µM. The comparison between the Km for ACC and the Ki for ACBC indicated that ACBC had an affinity which was ca. 5-fold higher than that of ACC. Whereas ACC inactivated carnation ACC oxidase in a time-dependent manner during incubation, ACBC did not cause the inactiva-tion of the enzyme. Preliminary experiments showed that ACBC and its N-substituted derivatives delayed the onset of senescence in cut carnation flowers.

(Received August 19, 1996; Accepted November 26, 1996)
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