Effects of chlorobenzoate transformation on the Pseudomonas testosteroni biphenyl and chlorobiphenyl degradation pathway
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.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
User Contributions:
Comment about this article or add new information about this topic:
Characterization of active recombinant 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni B-356 and sequence of the encoding gene (bphB)
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.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
User Contributions:
Comment about this article or add new information about this topic:
Metabolism of 2,2' - and 3,3' -dihydroxybiphenyl by the biphenyl catabolic pathway of Comamonas testosteroni B-356
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.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2004
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Genetic characterization of the phenylacetyl-coenzyme A oxygenase from the aerobic phenylacetic acid degradation pathway of Escherichia coli
- Abstracts: Maintenance and induction of naphthalene degradation activity in Pseudomonas putida and an Alacligenes sp. under different culture conditions
- Abstracts: Complete biological reductive transformation of tetrachloroethene to ethane. Transformation of low concentrations of 3-chlorobenzoate by Pseudomonas sp. strain B13: kinetics and residual concentrations
- Abstracts: Inference of horizontal genetic transfer from molecular data: an approach using the bootstrap. The evolution of insertion sequences within enteric bacteria
- Abstracts: Associations between nuclear loci and chloroplast DNA genotypes in wild barley. Nonrandom distribution of chloroplast recombination events in Chlamydomonas reinhardtii: evidence for a hotspot and an adjacent cold region