Nair, Madhusudanan P and Vaidyanathan, CS (1964) An indole oxidase isolated from the leaves of Tecoma stans. In: Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 81 (3). pp. 496-506.
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Abstract
The presence of an indole oxidase (indole: O2 oxidoreductase) was detected in the leaf extracts of Tecoma stans. The end product of the reaction was identified as anthranil. Formylaminobenzaldehyde, and o- aminobenzaldehyde were detected as intermediates in the overall conversion. Oxygen-uptake studies established that 3 atoms of oxygen were consumed in the formation of anthranil form I molecule of indole. The enzyme showed an absolute requirement for FAD and Cu2+ for maximum activity. FMN was ineffective as a cofactor. The enzyme had an optimum pH of 5.0. Inhibition studies with GSH and p-chloromericuribenzoate showed that a sulfhydrylcupric-ion complex at the active centre is highly essential.
| Item Type: | Journal Article |
|---|---|
| Additional Information: | Copyright of this article belongs to Elsevier Science. |
| Department/Centre: | Division of Biological Sciences > Biochemistry |
| Date Deposited: | 24 May 2010 07:27 |
| Last Modified: | 19 Sep 2010 06:07 |
| URI: | http://eprints.iisc.ernet.in/id/eprint/28083 |
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