Cucumber Seedling Indoleacetaldehyde Oxidase | Zendy

Peter Bower | Zendy; Hugh M. Brown | Zendy; William K. Purves | Zendy

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Cucumber Seedling Indoleacetaldehyde Oxidase

Author(s) -

Peter Bower,

Hugh M. Brown,

William K. Purves

Publication year - 1978

Publication title -

plant physiology

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.61.1.107

Subject(s) - phenylacetaldehyde , acetaldehyde , cucumis , indole test , enzyme , chemistry , biochemistry , substrate (aquarium) , benzaldehyde , indole 3 acetic acid , oxidase test , cofactor , seedling , stereochemistry , biology , botany , catalysis , auxin , ecology , gene , ethanol

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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