Metabolites formed during anaerobic transformation of toluene and o-xylene and their proposed relationship to the initial steps of toluene mineralization
Article Abstract:
Formation of metabolites in the anaerobic toluene and o-xylene microbial degradation shows incomplete transformation in the process. In this study, these metabolites wereidentified. Those simultaneously formed during toluene mineralization were identified by gas chromatography-mass spectrometry as benzylsuccinic acid and benzylfumaric acid. o-Xylene metabolites were likewise identified as (2- methylbenzyl)-succinic acid and (2-methylbenzyl)-fumaric acid. Transformation pathways were proposed based on experimental results on the role of succinic acid on o-xylene transformation and based on the transformation pathway that isresponsible for the transformation of toluene metabolites.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
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Identification and sequence analysis of two regulatory genes involved in anaerobic toluene metabolism by strain T1
Article Abstract:
The tutB and tutC gene products of mutant strains of T1 denitrifying bacterium correspond to members of two-component regulatory systems and are involved in anaerobic toluene metabolism. They are involved in the regulation of gene expression in response to toluene. The tutB mutants are unable to metabolize toluene and fail to generate significant amounts of dead-end products, benzylsuccinic acid and benzylfumaric acid. This indicates the presence of a common enzymatic step in the toluene metabolic pathways in the T1 strain.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
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Identification and analysis of genes involved in anaerobic toluene metabolism by strain T1: putative role of a glycine free radical
Article Abstract:
Two genes from the denitrifying strain T1 identified as tutD and tutE have been identified as components of the T1 toluene metabolic pathway. The gene product of tutD is homologous to pyruvate formate-lyase enzymes while that of tutE is homologous to pyruvate-lyase activating enzymes. Site directed mutagenesis was used to study and characterize the function of a conserved glycine residue at the active site of the tutD gene product.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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