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

IV. REGULATION

L. N. Ornston 1

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

Study of the regulation of the syntheses of enzymes of the catechol and protocatechuate pathways in Pseudomonas putida has shown that two groups of enzymes are subject to coordinate control. cis,cis-Muconate-lactonizing enzyme and muconolactone isomerase, which are uniquely associated with the catechol pathway, constitute the first coordinate block of enzymes. The synthesis of these enzymes, as well as that of catechol oxygenase (which is regulated independently), seems to be induced by cis,cis-muconate.

The second coordinate block of enzymes comprises ß-carboxy-cis,cis-muconate-lactonizing enzyme and gamma-carboxymuconolactone decarboxylase, which are uniquely associated with the protocatechuate pathway, and ß-ketoadipate enol-lactone hydrolase, which is functional in both the protocatechuate and the catechol pathways. This group of enzymes seems to be induced by ß-ketoadipate or ß-ketoadipyl coenzyme A.

Moraxella lwoffii, which degrades protocatechuate and catechol through identical step-reactions, regulates the synthesis of the enzymes mediating these conversions by a different mechanism.

Submitted on March 4, 1966


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