The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida.

L. Ornston,R. Stanier

Published 1966 in Journal of Biological Chemistry

ABSTRACT

SUMMARY Two new intermediates were identified in the protocatechuate pathway of Pseudomonas putida. The first of these, y - carboxymuconolactone (y -carboxy- y-carboxymethyl- A-butenolide), is the product of the enzymic lactonization of #-carboxy-cis, cis-muconate. Enzymic decarboxylation of y-carboxymuconolactone gives rise to -ketoadipate enol-lactone (y-carboxymethyl-A 5 -butenolide), the second newly discovered intermediate in the protocatechuate pathway. -Ketoadipate enol-lactone, which was isolated and physi-cally characterized, is also an intermediate in the catechol pathway; the catechol and protocatechuate pathways con-verge at this point. -Ketoadipate enol-lactone is hydrolyzed to P-ketoadipate an enzyme for utilization of either catechol or also degrades protocatechuate and catechol by the pathways characteristic of P. putida.

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