Subba Rao, PV and Vaidyanathan, CS (1967) Studies on the metabolism of o-aminophenol purification and properties of isophenoxazine synthase from Bauhenia monandra. In: Archives of Biochemistry and Biophysics, 118 (2). pp. 388-394.
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An enzyme which catalyzes the oxidative conversion of o-aminophenol to 2-amino-3-H-isophenoxazin-3-one has been purified 396-fold by using standard fractionation procedures. The enzyme is specific for o-aminophenol and has pH and temperature optima at 6.2 and 40 °, respectively. It is insensitive to metal chelating agents but is inhibited by several reducing substances. There is no cofactor or metal ion requirement for the reaction. A competitive type of inhibition was observed with structural analogs such as anthranilic acid and 3-hydroxyanthranilic acid. There are no free sulfhydryl groups in the enzyme, but preincubation of the enzyme with substrate or substrate analogs resulted in the liberation of titratable free sulfhydryl groups. The mechanism of biosynthesis of isophenoxazine ring is discussed.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||14 May 2010 05:38|
|Last Modified:||19 Sep 2010 06:06|
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