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Cucumber Seedling Indoleacetaldehyde Oxidase ¹

Biochemistry and Biophysics Section, Biological Sciences Group, University of Connecticut, Storrs, Connecticut 06268

Extracts of light-grown Cucumis sativus L. seedlings catalyzed the oxidation of indole-3-acetaldehyde to indole-3-acetic acid. No added cofactors were required. Inhibitor studies indicated that the enzyme is a metalloflavoprotein. While indole-3-aldehyde, benzaldehyde, and phenylacetaldehyde partially inhibited the oxidation of indole-3-acetaldehyde, suggesting that they may serve as alternative substrates, it is proposed that indoleacetaldehyde is the major substrate in vivo. 2,4-Dichlorophenoxyacetic acid strongly inhibited the indoleacetaldehyde oxidase activity, and it is proposed that this enzyme may be subject in vivo to feedback inhibition by indole-3-acetic acid. The enzyme was activated by brief heating or by treatment with mercaptoethanol.

³ Present address: Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403.

⁴ Present address: Biology Department, Harvey Mudd College, Claremont, California 91711.

¹ This work was supported by the University of Connecticut Research Foundation and by National Science Foundation Grant GB-40556 to W. K. P.

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