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.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Bower PJ,Brown HM,Purves WKdoi
10.1104/pp.61.1.107subject
Has Abstractpub_date
1978-01-01 00:00:00pages
107-10issue
1eissn
0032-0889issn
1532-2548journal_volume
61pub_type
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