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Plant Physiology 71:19-23 (1983)
© 1983 American Society of Plant Biologists

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Articles

Purification and Characterization of a New Indole Oxygenase from the Leaves of Tecoma stans L

Satya P. Kunapuli1 and Chelarkara S. Vaidyanathan

Enzymology and Plant Biochemistry Laboratory, Department of Biochemistry, Indian Institute of Science, Bangalore - 560 012, India

A new indole oxygenase from the leaves of Tecoma stans was isolated and purified to homogenity. The purified enzyme system catalyzes the conversion of indole to anthranilic acid. It is optimally active at pH 5.2 and 30°C. Two moles of oxygen are consumed and one mole of anthranilic acid is formed for every mole of indole oxidized. Dialysis resulted in complete loss of the activity. The inactive enzyme could be reactivated by the addition of concentrated dialysate. The enzyme is not inhibited by copper-specific chelators, non-heme iron chelators or atebrin. It is not a cuproflavoprotein, unlike the other indole oxygenases and oxidases.

1 To whom reprint requests should be sent. Present address: Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78284.






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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1983 by the American Society of Plant Biologists