Isophenoxazine synthase


Autoria(s): Nair, Madhusudanan P; Vaidyanathan, CS
Data(s)

09/03/1964

Resumo

An enzyme which catalyses the oxidation of o-aminophenol to o-quinoneimine and the subsequent condensation of o-aminophenol and o-quinoneime to give isophenoxazine has been isolated from the leaves of Tecoma stans. The reaction had an optimum pH of 6.2 and an optimum temperature of 45°. Heavy-metal ions like Hg2+, Co2+, Mg2+, Fe3+, were inhibitory. Mn2+ activated the reaction to about 40%. The reaction requires intact sulfhydryl groups. A study of the coenzyme requirements showed that isophenoxazine synthase (o-aminophenol: O2 oxidoreductase) is a flavoprotein requiring FAD for maximum activity. Stoichiometric studies showed that 2 moles of o-aminophenol gave 1 mole of isophhenoxazine.

Formato

application/pdf

Identificador

http://eprints.iisc.ernet.in/28085/1/ISO.pdf

Nair, Madhusudanan P and Vaidyanathan, CS (1964) Isophenoxazine synthase. In: Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 81 (3). pp. 507-516.

Publicador

Elsevier Science

Relação

http://dx.doi.org/10.1016/0926-6569(64)90135-X

http://eprints.iisc.ernet.in/28085/

Palavras-Chave #Biochemistry
Tipo

Journal Article

PeerReviewed