Abstract
Summary The plant hormone ethylene regulates senescence in carnation flowers. The final step in the biosynthesis of ethylene i.e. the conversion of ACC to ethylene is catalysed by the enzyme ACC oxidase. ACC oxidase was extracted from carnation petals and its characteristics were determined. The enzyme appears to be a soluble enzyme and requires Fe 2+ and ascorbate for maximal activity. CO 2 increases the reaction velocity and the apparent K m for ACC from 30 µM to 425 µM. Both Co 2+ and the ACC analog α-aminoisobutyric acid inhibit the ACC oxidase activity. The change in in vivo ACC oxidase activity in senescing carnation flowers is accompanied by a parallel change in ACC oxidase mRNA abundance and in vitro ACC oxidase activity. Optimal conditions for extraction and determination of authentic carnation petal ACC oxidase activity in vitro are described.
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