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

II. ENZYMES OF THE PROTOCATECHUATE PATHWAY

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

Purification procedures for four enzymes of the protocatechuate pathway were described. Protocatechuate oxygenase was separated from ß-carboxy-cis,cis-muconate-lactonizing enzyme by Sephadex G-200 filtration. Alumina C gel was used to separate ß-carboxy-cis,cis-muconate lactonizing enzyme from -carboxymuconolactone decarboxylase. These two enzymes were also separated by diethylaminoethyl cellulose chromatography. ß-Ketoadipate enol-lactone hydrolase was removed from solutions of -carboxymuconolactone decarboxylase by heat treatment. ß-Ketoadipate enol-lactone hydrolase was greatly purified by DEAE-cellulose chromatography and Sephadex G-100 filtration.

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