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Plant Physiology 86:868-872 (1988)
© 1988 American Society of Plant Biologists

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Metabolism and Enzymology

Oxidation of Indole-3-Acetic Acid to Oxindole-3-Acetic Acid by an Enzyme Preparation from Zea mays1

Dennis M. Reinecke and Robert S. Bandurski

Department of Botany and Plant Pathology, Michigan State University, East Lansing, Michigan 48824

Indole-3-acetic acid is oxidized to oxindole-3-acetic acid by Zea mays tissue extracts. Shoot, root, and endosperm tissues have enzyme activities of 1 to 10 picomoles per hour per milligram protein. The enzyme is heat labile, is soluble, and requires oxygen for activity. Cofactors of mixed function oxygenase, peroxidase, and intermolecular dioxygenase are not stimulatory to enzymic activity. A heat-stable, detergent-extractable component from corn enhances enzyme activity 6- to 10-fold. This is the first demonstration of the in vitro enzymic oxidation of indole-3-acetic acid to oxindole-3-acetic acid in higher plants.

1 Supported by a National Aeronautics and Space Administration (NASA) Graduate Researcher's Program award to D. M. R. and by grants from the Metabolic Biology Section of the National Science Foundation, DMB 8504231, and by the Space Biology Section of NASA, NAGW-97 and NAG2-362 to R. S. B.






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Copyright © 1988 by the American Society of Plant Biologists