THE BACTERIAL DEGRADATION OF CATECHOL

Abstract
Two strains of Pseudomonas grown with phenol were used to prepare cell extracts that metabolized catechol with the transient formation of 2-hydroxymuconic semialdehyde. One of these preparations catalyzed the conversion of 1 mole of catechol into 1 mole each of formate and 4-hydroxy-2-oxovalerate. A method for the determination of 4-hydroxy-2-oxovalerate is described, together with some properties of this compound and its 2,4-dinltrophenylhydrazone. Another partially purified cell extract converted 1 mole of 4-hydroxy-2-oxovalerate, formed enzymically from catechol, into 1 mole each of acetaldehyde and pyruvate. The aldolase had a pH optimum of about 8.8, was stimulated by Mg2+ ions and attacked only 1 enantiomer of synthetic 4-hydroxy-2-oxovalerate.