Kunapuli, Satya P. ; Vaidyanathan, Chelarkara S. (1983) Purification and characterization of a new indole oxygenase from the leaves of Tecoma stans L. Plant Physiology, 71 (1). pp. 19-23. ISSN 0032-0889
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Official URL: http://www.plantphysiol.org/content/71/1/19.full.p...
Related URL: http://dx.doi.org/10.1104/pp.71.1.19
Abstract
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.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to American Society of Plant Biologists. |
| ID Code: | 77265 |
| Deposited On: | 10 Jan 2012 14:08 |
| Last Modified: | 10 Jan 2012 14:08 |
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