R. Blasco et al., FROM XENOBIOTIC TO ANTIBIOTIC, FORMATION OF PROTOANEMONIN FROM 4-CHLOROCATECHOL BY ENZYMES OF THE 3-OXOADIPATE PATHWAY, The Journal of biological chemistry, 270(49), 1995, pp. 29229-29235
Chloroaromatics, a major class of industrial pollutants, may be oxidat
ively metabolized to chlorocatechols by soil and water microorganisms
that have evolved catabolic activities toward these xenobiotics. We sh
ow 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-mucona
te 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.