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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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|
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