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Elsevier, Journal of Biological Chemistry, 49(270), p. 29229-29235, 1995

DOI: 10.1074/jbc.270.49.29229

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From xenobiotic to antibiotic, formation of protoanemonin from 4-Chlorocatechol by enzymes of the 3-Oxoadipate pathway

This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Chloroaromatics, a major class of industrial pollutants, may be oxidatively metabolized to chlorocatechols by soil and water microorganisms that have evolved catabolic activities toward these xenobiotics. We show here that 4-chlorocatechol can be further transformed by enzymes of the ubiquitous 3-oxoadipate pathway. However, whereas chloromuconate cycloisomerases catalyze the dechlorination of 3-chloro-cis,cis-muconate to form cis-dienelactone, muconate cycloisomerases catalyze a novel reaction, i.e. the dechlorination and concomitant decarboxylation to form 4-methylenebut-2-en-4-olide (protoanemonin), an ordinarily plant-derived antibiotic that is toxic to microorganisms.