Abstract
1-Aminocyclopropane-1-carboxylic acid (ACC) oxidase, the enzyme that catalyzes the final step in ethylene biosynthesis, was recovered from pear (Pyrus communis L. cv. Blanquilla) fruit tissues with maximum activity at pH 6.5. The enzyme eluted as a single hydrophobic protein with an estimated molecular weight of 37.9 kDa in a three-step FPLC chromatographic procedure. The sensitivity of the pear ACC oxidase against a range of chemicals known by their inhibitory action on ethylene biosynthesis in vivo has been studied. Among them, and in contrast to a previous proposal, α-(p-chlorophenoxy)isobutyric acid, a substance possessing antiauxin properties, did not inhibit the in vitro enzyme activity. The significance of the results is discussed in terms of the nature and mechanism of the enzyme reaction.
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