Journal Article

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

Yusuke Kosugi, Naoko Oyamada, Shigeru Satoh, Toshihito Yoshioka, Ei-ichi Onodera and Yuko Yamada

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 38, issue 3, pages 312-318
Published in print January 1997 | ISSN: 0032-0781
Published online January 1997 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029168
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

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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.

Keywords: 1-Aminocyclobutane-l-carboxylate (ACBC); 1-Aminocyclopropane-l-carboxylate (ACC) oxidase; Carnation (Dianthus caryophyllus L.); Competitive inhibition; Ethylene production; Flower longevity

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Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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