In vivo reactivation of catechol 2,3-dioxygenase mediated by a chloroplast-type ferredoxin: a bacterial strategy to expand the substrate specificity of aromatic degradative pathways.

摘要: The meta-cleavage operon of the TOL plasmid pWW0 Pseudomonas putida contains 13 genes responsible for oxidation benzoate and toluates to Krebs cycle intermediates via estradiol (meta) cleavage (methyl)catechol. functions all are known with exception xylT. We constructed mutants defective in xylT gene, found that these were not able grow on p-toluate while they still capable growing m-toluate. In mutants, enzymes induced by catechol 2,3-dioxygenase whose activity was 1% p-toluate-induced wild-type cells. Addition 4-methylcatechol m-toluate-grown cells resulted inactivation strain but mutant, regenerated a short time. regeneration also observed H2O2-treated cells, concluded product is required 2,3-dioxygenase.