Article Abstract:
Transformation of chlorobenzoates (CBAs) from biphenyl (BP) and chlorobiphenyls (CBPs) is mediated by bacterial degradation. Pseudomonas testosteroni demonstrates the metabolic interactions that occur within the BP degradation pathway. Metabolites are produced that prevent complete mineralization of CBPs. One particular metabolite is 3CBA which is themost effective inhibitor of the BP pathway. Other metabolites are chlorocatechols and semialdehydes. Genetic manipulations are needed to prevent CBA-degrading enzymes from producing these inhibitory metabolites.
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Article Abstract:
Sequence analysis of Comamonas testosteroni strain B-356 bphB shows that 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase (B2,3D) is as active as other bacterial strains in its ability to degrade polychlorinated biphenyl (PCB) congeners. B2,3D requires NAD+, an optimal pH of 9.5, and a native M(sub r) of 123, 000. These features are similar to those of the related molecule cis-toluene dihydrodiol dehydrogenase. However, unlike cis-toluene dihydrodiol dehydrogenase, pattern B356 B2,3D is unable to transform cis-1,2-dihydroxycyclohexa-3,5-diene.
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Article Abstract:
Results indicate that between the two dihydroxybiphenyls, 3,3'-dihydroxybiphenyl is the preferred substrate for the biphenyl catabolic enzymes of Comamonas testosteroni B-356. Data show that in the metabolic pathway of the dihydroxybiphenyls, the major step is a direct dehydroxylation of one of the ortho-substituted carbons yielding 2,3,2'-trihydroxybiphenyl.
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