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Main Title Mutants of 'Pseudomonas cepacia' G4 Defective in Catabolism of Aromatic Compounds and Trichloroethylene.
Author Shields, M. S. ; Montgomery, S. O. ; Cuskey, S. M. ; Chapman., P. J. ;
CORP Author Environmental Research Lab., Gulf Breeze, FL.
Publisher c1991
Year Published 1991
Report Number EPA/600/J-91/337 ;CONTRIB-730;
Stock Number PB92-129741
Additional Subjects Mutations ; Toluene ; Trichloroethylene ; Aromatic compounds ; Metabolism ; Catalysis ; Mutagenesis ; Gas chromatography ; Phenotype ; Hydroxylation ; Oxidation ; Biodeterioration ; Reprints ; Pseudomonas cepacia
Library Call Number Additional Info Location Last
NTIS  PB92-129741 Some EPA libraries have a fiche copy filed under the call number shown. 07/26/2022
Collation 9p
Pseudomonas cepacia G4 possesses a novel pathway of toluene catabolism that is shown to be responsible for the degradation of trichloroethylene (TCE). The pathway involves conversion of toluene via o-cresol to 3-methylcatechol. In order to determine the enzyme of toluene degradation that is responsible for TCE degradation, chemically induced mutants, blocked in the toluene ortho-monooxygenase (TOM) pathway of G4, were examined. Mutants of the phenotypic class designated TOM A(-) were all defective in their ability to oxidize toluene, o-cresol, m-cresol, and phenol, suggesting that a single enzyme is responsible for conversion of these compounds to their hydroxylated products (3-methylcatechol from toluene, o-cresol, and m-cresol and catechol from phenol) in the wild type. Mutants of this class did not degrade TCE. Two other mutant classes which were blocked in toluene catabolism, TOM B(-), which lacked catechol-2,3-dioxygenase, and TOM C(-) which lacked 2-hydroxy-6-oxoheptadienoic acid hydrolase activity, were fully capable of TCE degradation. Therefore, TCE degradation is directly associated with the monooxygenation capability responsible for toluene, cresol, and phenol hydroxylation. (Copyright (c) 1991, American Society for Microbiology.)