3-(2-hydroxyphenyl)catechol as substrate for proximal meta ring cleavage in dibenzofuran degradation by Brevibacterium sp. strain DPO 1361

@article{Strubel199132hydroxyphenylcatecholAS,
  title={3-(2-hydroxyphenyl)catechol as substrate for proximal meta ring cleavage in dibenzofuran degradation by Brevibacterium sp. strain DPO 1361},
  author={V. Strubel and K. Engesser and P. Fischer and H. Knackmuss},
  journal={Journal of Bacteriology},
  year={1991},
  volume={173},
  pages={1932 - 1937}
}
Brevibacterium sp. strain DPO 1361 oxygenates dibenzofuran in the unusual angular position. The 3-(2-hydroxyphenyl)catechol thus generated is subject to meta ring cleavage in the proximal position, yielding 2-hydroxy-6-(2-hydroxyphenyl)-6-oxo-2,4-hexadienoic acid, which is hydrolyzed to 2-oxo-4-pentenoate and salicylate by 2-hydroxy-6-oxo-6-phenyl-2,4-hexadienoic acid hydrolase. The proximal mode of ring cleavage is definitely established by isolation and unequivocal structural characterization… Expand
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References

SHOWING 1-10 OF 21 REFERENCES
Purification and some properties of a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolyzing enzyme from Pseudomonas cruciviae S93 B1 involved in the degradation of biphenyl
Pseudomonas cruciviae S93B1 produced three HOPDA reducing enzymes (I, II, III), found by chromatography on DEAE-Sepharose CL-6B. The purified HOPDA reducing enzyme III was homogeneous onExpand
Purification and Some Properties of the 2-Hydroxy-6-oxohepta-2,4-dienoate Hydrolase (2-Hydroxymuconic Semialdehyde Hydrolase) Encoded by the TOL Plasmid pWW0 from Pseudomonas putida mt-2
TLDR
Kinetic measurements showed that the higher activity against the ketone substrates over aldehyde substrates (from 3-substituted catechols) was the result of higher V max values rather than lower K m values, and this was related to the HOD hydrolase from phenol-grown P. putida strain U. Expand
Dioxygenolytic cleavage of aryl ether bonds: 1,10-dihydro-1,10-dihydroxyfluoren-9-one, a novel arene dihydrodiol as evidence for angular dioxygenation of dibenzofuran.
TLDR
Two dibenzofuran degrading bacteria were found to utilize fluorene as sole source of carbon and energy and the presence of a novel type of dioxygenase, attacking polynuclear aromatic systems in the unusual angular position was indicated. Expand
Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol
TLDR
Kinetic analyses revealed that 2,3-dioxygenase preparations from toluene-grown cells of Pseudomonas putida catalyzed the stoichiometric oxidation of 3-methylcatechol to 2-hydroxy-6-oxohepta-2,4-dienoate and 3-chlorocatechol were noncompetitive or mixed-type inhibitors of the enzyme. Expand
Stereospecific Enzymes in the Degradation of Aromatic Compounds by Pseudomonas putida
TLDR
It was demonstrated that l-(S)-4-hydroxy-2-oxohexanoate is the biologically active enantiomer of this hydroxy acid, and a mechanism is proposed which closely resembles that for 4-Hydroxy- 2-oxopentanoate aldolase. Expand
Degradation of 2-bromo-, 2-chloro- and 2-fluorobenzoate by Pseudomonas putida CLB 250.
TLDR
After inhibition of ring cleavage activities with 3-chlorocatechol, 2-chlorobenzoate was transformed to catechol in nearly stoichiometric amounts and other ortho-substituted benzoates like anthranilate and 2-methoxybenzoate seem to be metabolized via the same route. Expand
Bacterial communities degrading amino- and hydroxynaphthalene-2-sulfonates
A 6-aminonaphthalene-2-sulfonic acid (6A2NS)-degrading mixed bacterial community was isolated from a sample of river Elbe water. The complete degradation of this xenobiotic compound may be describedExpand
Transformation of Dibenzo-p-Dioxin by Pseudomonas sp. Strain HH69
Dibenzo-p-dioxin was oxidatively cleaved by the dibenzofuran-degrading bacterium Pseudomonas sp. strain HH69 to produce minor amounts of 1-hydroxydibenzo-p-dioxin and catechol, while a 2-phenoxyExpand
Metabolism of Dibenzofuran by Pseudomonas sp. Strain HH69 and the Mixed Culture HH27
TLDR
Evidence is given for a novel type of dioxygenases responsible for the attack on the biarylether structure of the dibenzofuran molecule and a meta-fission mechanism for cleavage of the dihydroxylated aromatic nucleus of 2,2',3-trihydroxybiphenyl is suggested as the next enzymatic step in the degradative pathway. Expand
Enrichment of dibenzofuran utilizing bacteria with high co-metabolic potential towards dibenzodioxin and other anellated aromatics.
TLDR
High rates of co-oxidation of dibenzodioxin demonstrate analogue-enrichment to be a powerful technique for selecting enzymatic activities for otherwise non-degradable substrates. Expand
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