Catabolism of pseudocumene and 3-ethyltoluene by Pseudomonas putida (arvilla) mt-2: evidence for new functions of the TOL (pWWO) plasmid

Kunz, Daniel A.; Chapman, P. J.

doi:10.1128/jb.146.1.179-191.1981

Cited by 130 publications

(51 citation statements)

References 39 publications

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“…A 12-kg soil sample, used to select the bacterial culture analysed in the study, was collected at a depth of 18 m as an undisturbed core during the installation of vacuum wells of a bioventing plant for the bioremediation of the soil contaminated by BTEX (benzene, toluene, ethylbenzene and xylenes) and naphtha solvent from the grounds of a paint factory. A total of 50 g of soil was mixed with 450 ml of sterile NaCl solution (9 g l À1 ) and shaken for 2 h at 30 C. The soil suspension (10 ml) was seeded in a¯ask containing 200 ml of M9 mineral medium (Kunz and Chapman 1981) supplemented with 250 mg l À1 of naphtha solvent and incubated at 30 C for 7 d on an alternative shaker. The culture was adapted to degrade the aromatic mixture by re-inoculating 1 ml of the cell suspension in 20 ml of M9 mineral medium supplemented with 250 mg l À1 of naphtha solvent and then incubated at 30 C. The adapted cells were subjected to 10 subsequent passages.…”

Section: Enrichment Proceduresmentioning

confidence: 99%

Evolution of a degradative bacterial consortium during the enrichment of naphtha solvent

et al. 2000

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A microbial mixed culture able to degrade naphtha solvent, a model of hydrocarbon aromatic mixture, was isolated from a hydrocarbon‐polluted soil. Composition of the population was monitored by phenotypic and molecular methods applied on soil DNA, on whole enrichment culture DNA, and on 85 isolated strains. Strains were characterized for their 16S rDNA restriction profiles and for their random amplified polymorphic DNA profiles. Catabolic capabilities were monitored by phenotypic traits and by PCR assays for the presence of the catabolic genes methyl mono‐oxygenase ( xylA,M), catechol 2,3 dioxygenase (xylE) and toluene dioxygenase (todC1) of TOL and TOD pathways. Different haplotypes belonging to Pseudomonas putida, Ps. aureofaciens and Ps. aeruginosa were found to degrade aromatic compounds and naphtha solvent. The intrinsic catabolic activity of the microbial population of the polluted site was detected by PCR amplification of the xylE gene directly from soil DNA.

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Section: Enrichment Proceduresmentioning

confidence: 99%

Evolution of a degradative bacterial consortium during the enrichment of naphtha solvent

et al. 2000

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“…PaW1 expresses a xylene monooxygenase which oxidizes alkyl substituents rather than the aromatic ring. This enzyme mediates the initial hydroxylation step in the pathways for the utilization of TOL, m-and p-xylene, and 1,2,4-TMB [26,40], and co-oxidizes both 1,3,5-TMB and STYR [41]. PaW1 degraded these and only these compounds in hydrocarbon mixtures in the present study, probably because none of the other aromatic compounds bore suitable substituents, and PaW1 has not been shown to oxidize chloroaliphatic hydrocarbons.…”

Section: Resultsmentioning

confidence: 61%

Degradation of mixtures of aromatic and chloroaliphatic hydrocarbons by aromatic hydrocarbon-degrading bacteria

Leahy¹

2003

FEMS Microbiology Ecology

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The well-characterized toluene-oxidizing bacteria Pseudomonas putida PaW1, P. putida F1, P. mendocina KR1, Burkholderia cepacia G4, B. cepacia JS150, and Ralstonia pickettii PKO1, as well as several strains of bacteria isolated from activated sludge, were examined for their ability to degrade mixtures of aromatic and chloroaliphatic hydrocarbons. Collectively, the strains tested were able to transform all of the 14 aromatic hydrocarbons included in the mixtures, with most strains degrading five or more. Few strains degraded trichloroethylene well under these conditions, only one degraded methylene chloride, and none were able to transform chloroform. G4, PKO1, KR1, F1, and JS150 exhibited generally broad but oxygenase-specific degradation profiles, with the three monooxygenase strains degrading significantly more o-xylene and trichloroethylene, and F1 and JS150 degrading greater quantities of isopropylbenzene and 1,4dichlorobenzene. PaW1 degraded only the methylaromatic hydrocarbons and styrene. Sludge isolates enriched on benzene, toluene, styrene and the xylenes exhibited degradation profiles similar to F1 or PaW1, while the pattern of hydrocarbon degradation for the ethylbenzene, isopropylbenzene, 1,3,5-trimethylbenzene, and 1,3-dichlorobenzene isolates were distinct from the other strains and from each other. Overall, our results showed that many of the bacteria which utilize aromatic compounds are capable of degrading a diverse array of aromatic hydrocarbons in mixtures, but that chloroaliphatics such as methylene chloride and chloroform may be recalcitrant to co-oxidation in the presence of aromatics or trichloroethylene.

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“…2. Dihydroxylation of a particular substrate by the enzyme produces its corresponding catechol, which undergoes auto-oxidation to form colored compounds, indicating activity against that substrate [22,27,31,32].…”

Section: Substrate Specificity Of Atdamentioning

confidence: 99%

Probing the molecular determinants of aniline dioxygenase substrate specificity by saturation mutagenesis

2007

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Aniline dioxygenase is a multicomponent Rieske nonheme‐iron dioxygenase enzyme isolated from Acinetobacter sp. strain YAA. Saturation mutagenesis of the substrate‐binding pocket residues, which were identified using a homology model of the α subunit of the terminal dioxygenase (AtdA3), was used to probe the molecular determinants of AtdA substrate specificity. The V205A mutation widened the substrate specificity of aniline dioxygenase to include 2‐isopropylaniline, for which the wild‐type enzyme has no activity. The V205A mutation also made 2‐isopropylaniline a better substrate for the enzyme than 2,4‐dimethylaniline, a native substrate of the wild‐type enzyme. The I248L mutation improved the activity of aniline dioxygenase against aniline and 2,4‐dimethylaniline approximately 1.7‐fold and 2.1‐fold, respectively. Thus, it is shown that the α subunit of the terminal dioxygenase indeed plays a part in the substrate specificity as well as the activity of aniline dioxygenase. Interestingly, the equivalent residues of V205 and I248 have not been previously reported to influence the substrate specificity of other Rieske dioxygenases. These results should facilitate future engineering of the enzyme for bioremediation and industrial applications.

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Catabolism of pseudocumene and 3-ethyltoluene by Pseudomonas putida (arvilla) mt-2: evidence for new functions of the TOL (pWWO) plasmid

Cited by 130 publications

References 39 publications

Evolution of a degradative bacterial consortium during the enrichment of naphtha solvent

Evolution of a degradative bacterial consortium during the enrichment of naphtha solvent

Degradation of mixtures of aromatic and chloroaliphatic hydrocarbons by aromatic hydrocarbon-degrading bacteria

Probing the molecular determinants of aniline dioxygenase substrate specificity by saturation mutagenesis

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