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J Bacteriol. 1973 February; 113(2): 922-931
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

Stereospecific Enzymes in the Degradation of Aromatic Compounds by Pseudomonas putida

¹ Department of Biochemistry, St. Paul Campus, University of Minnesota, St. Paul, Minnesota 55101

ABSTRACT

Two reactions in the catabolism of catechol by meta-fission, namely, hydration of 2-oxopent-4-enoate (vinylpyruvate) and aldol fission of the product, are catalyzed by stereospecific enzymes. The absolute configuration of this hydration product was shown to be L(S)-4-hydroxy-2-oxopentanoate. Vinylpyruvate hydratase, purified almost to homogeneity, had a molecular weight of about 287,000 and was dissociated in sodium dodecyl sulfate, without prior treatment with mercaptoethanol, into a species with an approximate molecular weight of 28,000. The hydratase was highly specific for its substrates; thus, although 2-oxo-cis-hex-4-enoate was also hydrated, structurally similar compounds such as the trans isomer, vinylacetic and crotonic acids, and the ring-fission products of catechol and methylcatechols were not attacked. Vinylpyruvate hydratase was activated by Mn²⁺ ions. On the basis of these observations, a mechanism is proposed which closely resembles that for 4-hydroxy-2-oxopentanoate aldolase. A possible evolutionary connection between functionally related, divalent cation-activated hydro-lyases and aldolases is discussed. It was also demonstrated that L-(S)-4-hydroxy-2-oxohexanoate is the biologically active enantiomer of this hydroxy acid.

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