Hybrid pathway for chlorobenzoate metabolism in Pseudomonas sp. B13 derivatives

Abstract

Derivatives of Pseudomonas sp. B13 which acquired the capability to utilize 4-chloro- and 3,5-dichlorobenzoate as a consequence of the introduction of genes of the TOL plasmid of P. putida mt-2 were studied. The utilization of these substrates, a property not shared by the parent strains, depended upon the combined activities of enzymes from the donor and from the recipient. During growth on 3-chloro-, 4-chloro- and 3,5-dichlorobenzoate, predominantly the toluate 1,2-dioxygenase and both dihydrodihydroxybenzoate dehydrogenases of the parent strains were induced. No catechol 2,3-dioxygenase from P. putida mt-2 was detectable, so that degradation of chlorocatechols by the nonproductive meta-cleavage pathway was avoided. Instead of that, chlorocatechols were subject to ortho cleavage and totally degraded by the preexisting enzymes of Pseudomonas sp. B13.