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Abstract
An aryl alcohol dehydrogenase (aryl alcohol: NADP +oxidoreductase. EC 1.1.1.91), that catalyzes the interconversion of benzyl alcohol and benzaldehyde as well as the oxidation of p- aminobenzyl alcohol has been isolated from Mycobacterium tuberculosis cells (American Type Culture Collection No. 607) grown in the presence of p- aminobenzoic acid. The partially purified enzyme shows a major peak with a minor contaminating component upon ultracentrifugation. The enzyme shows a broad substrate specificity and is sensitive to the buffer composition. The enzyme is inhibited by p- chloromercuribenzoate and 1,10-o- phenanthroline . The apparent K m values and the calculation of the approximate equilibrium constant are also presented.
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