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. 1978 Jan;61(1):107–110. doi: 10.1104/pp.61.1.107

Cucumber Seedling Indoleacetaldehyde Oxidase 1

Peter J Bower 1,2, Hugh M Brown 1,3, William K Purves 1,4
PMCID: PMC1091807  PMID: 16660220

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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