Purification and Characterization of Catechol 1, 2-Dioxygenase from Aniline-assimilating Rhodococcus erythropolis AN-13

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Catechol 1, 2-dioxygenase (EC 1.13.11.1) was purified to homogeneity from a cell-free extract of aniline-grown Rhodococcus erythropolis AN-13. The purified enzyme was stable between pH 7.0 and 10.5 and up to 40°C. The optimal pH was 7.5 for catechol as a substrate. The molecular weight of the enzyme was 37, 000 by gel filtration and 36, 000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This enzyme contained 3mol of sulfhydryl groups per mol of protein, but not disulfide bonds of cystine residues. The enzymatic activity was inhibited by AgNO3, HgCl2, iodoacetic acid and p-chloromercuribenzoic acid. FeSO4 and FeCl3 also inhibited the activity, although the enzyme contained 1.3g atoms of iron per mol of protein. This enzyme catalyzed the intradiol cleavage of 3- and 4-methylcatechol, but not the extradiol cleavage of 3-methylcatechol.
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