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The Conversion of Catechol and Protocatechuate to ß-Ketoadipate by Pseudomonas putida

III. ENZYMES OF THE CATECHOL PATHWAY

From the ¹ From the Department of Bacteriology and Immunology, University of California, Berkeley, California 94720

Extracts of benzoate-grown Pseudomonas putida have high levels of ß-carboxy-cis,cis-muconate-lactonizing enzyme and -carboxymuconolactone decarboxylase, even though these enzymes are uniquely associated with the protocate-chuate pathway. Since these activities might result from nonspecific catalysis by the enzymes which catalyze the analogous reactions in the catechol pathway, cis,cis-muconate-lactonizing enzyme and muconolactone isomerase were purified extensively and their specificities were examined. Crystalline preparations had no detectable activity on the carboxylated substrate analogues of the parallel convergent pathway. The enzymes of the catechol pathway do, however, share some physical characteristics with the enzymes that catalyze the analogous reactions in the protocatechuate pathway.

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