Purification and characterization of 6-chlorohydroxyquinol 1,2-dioxygenase from Streptomyces rochei 303: comparison with an analogous enzyme from Azotobacter sp. strain GP1
@article{Zaborina1995PurificationAC, title={Purification and characterization of 6-chlorohydroxyquinol 1,2-dioxygenase from Streptomyces rochei 303: comparison with an analogous enzyme from Azotobacter sp. strain GP1}, author={Olga E. Zaborina and Mark Latus and J{\"u}rgen Ebersp{\"a}cher and Ludmila A. Golovleva and Franz Lingens}, journal={Journal of Bacteriology}, year={1995}, volume={177}, pages={229 - 234} }
The enzyme which cleaves the benzene ring of 6-chlorohydroxyquinol was purified to apparent homogeneity from an extract of 2,4,6-trichlorophenol-grown cells of Streptomyces rochei 303. Like the analogous enzyme from Azotobacter sp. strain GP1, it exhibited a highly restricted substrate specificity and was able to cleave only 6-chlorohydroxyquinol and hydroxyquinol and not catechol, chlorinated catechols, or pyrogallol. No extradiol-cleaving activity was observed. In contrast to 6…
63 Citations
Purification and Characterization of Hydroxyquinol 1,2-Dioxygenase from Azotobacter sp. Strain GP1
- Chemistry, BiologyApplied and environmental microbiology
- 1995
Hydroxyquinol 1,2-dioxygenase was purified from cells of the soil bacterium Azotobacter sp. strain GP1 grown with 2,4,6-trichlorophenol as the sole source of carbon. The presumable function of this…
Purification and Characterization of 2 , 4 , 6-Trichlorophenol-4-Monooxygenase , a Dehalogenating Enzyme from Azotobacter sp . Strain GP 1
- Biology, Chemistry
- 1996
The enzyme which catalyzes the dehalogenation of 2,4,6-trichlorophenol (TCP) was purified to apparent homogeneity from an extract of TCP-induced cells of Azotobacter sp. strain GP1. The initial step…
Purification and characterization of 2,4,6-trichlorophenol-4-monooxygenase, a dehalogenating enzyme from Azotobacter sp. strain GP1
- Biology, ChemistryJournal of bacteriology
- 1997
The enzyme which catalyzes the dehalogenation of 2,4,6-trichlorophenol (TCP) was purified to apparent homogeneity from an extract of TCP-induced cells of Azotobacter sp. strain GP1. The initial step…
Purification and characterization of 2,6-dichloro-p-hydroquinone chlorohydrolase from Flavobacterium sp. strain ATCC 39723
- BiologyJournal of bacteriology
- 1997
The enzyme converted 2,6-DiCH to 6-chlorohydroxyquinol (6-chloro-1,2,4-trihydroxybenzene), which was easily oxidized by molecular oxygen and hard to detect and was detected only in the presence of a reductase and NADH in the reaction mixture.
Purification and Characterization of 2,6-Dichloro- p -Hydroquinone Chlorohydrolase from Flavobacterium sp. Strain ATCC 39723
- Biology
- 1997
The purified enzyme converted 2,6-DiCH to 6-chlorohydroxyquinol (6-chloro-1,2,4- trihydroxybenzene), which was easily oxidized by molecular oxygen and hard to detect.
Protein purification and genetic characterization of a streptomycete protocatechuate 3,4-dioxygenase
- Biology
- 1999
A previously uncharacterized Streptomyces sp. isolate 2065 was found to degrade vanillic acid and jc-hydroxybenzoic acid, utilizing these compounds as a sole carbon source. Induction of…
Cloning and sequence analysis of hydroxyquinol 1,2-dioxygenase gene in 2,4,6-trichlorophenol-degrading Ralstonia pickettii DTP0602 and characterization of its product.
- Biology, ChemistryJournal of bioscience and bioengineering
- 1999
Crystallization and preliminary crystallographic analysis of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E: a novel dioxygenase involved in the biodegradation of polychlorinated aromatic compounds.
- ChemistryActa crystallographica. Section D, Biological crystallography
- 1999
This is the first intradiol dioxygenase which specifically catalyzes the cleavage of hydroxyquinol to give diffraction-quality crystals, and the enzyme is an homodimer composed of two identical subunits in a alpha 2-type quaternary structure.
Characterization of the Maleylacetate Reductase MacA of Rhodococcus opacus 1CP and Evidence for the Presence of an Isofunctional Enzyme
- BiologyJournal of bacteriology
- 1998
The gene macA, which codes for one of apparently (at least) two maleylacetate reductases in the gram-positive, chlorophenol-degrading strain Rhodococcus opacus 1CP, is cloned and it is shown that it clearly is not part of a specialized chlorocatechol gene cluster.
Cloning of a gene encoding hydroxyquinol 1,2-dioxygenase that catalyzes both intradiol and extradiol ring cleavage of catechol.
- Biology, ChemistryBioscience, biotechnology, and biochemistry
- 1999
Results showed that the hydroxyquinol 1,2-dioxygenase reported here was a novel dioXYgenase that catalyzed both the intradiol and extradiol cleavage of catechol.
References
SHOWING 1-10 OF 42 REFERENCES
Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance.
- BiologyBiochemistry
- 1991
It is shown here that purified chlorocatechol dioxygenase from Pseudomonas putida is able to oxygenate a wide range of substituted catechols with turnover numbers ranging from 2 to 29 s-1, suggesting a highly conserved catalytic site.
Purification and characterization of a 1,2,4-trihydroxybenzene 1,2-dioxygenase from the basidiomycete Phanerochaete chrysosporium
- Biology, EngineeringJournal of bacteriology
- 1994
THB dioxygenase catalyzes a key step in the degradation pathway of vanillate, an intermediate in lignin degradation, and is reduced to beta-ketoadipate by an NADPH-requiring enzyme present in partially purified extracts.
Chemical structure and biodegradability of halogenated aromatic compounds. Two catechol 1,2-dioxygenases from a 3-chlorobenzoate-grown pseudomonad.
- BiologyThe Biochemical journal
- 1978
1. Two catechol 1,2-dioxygenases, pyrocatechase I and pyrocatechase II, were found in 3-chlorobenzoate-grown cells of Pseudomonas sp. B 13. The latter enzyme showed high relative activities with 3-…
Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4)
- BiologyJournal of bacteriology
- 1993
Results and the kinetic parameters suggest that the maleylacetate reductase is sufficient to channel the 2,4-D degradation intermediate 2-chloromaleylacetates into the 3-oxoadipate pathway.
2,4-D metabolism: pathway of degradation of chlorocatechols by Arthrobacter sp.
- Chemistry, BiologyJournal of agricultural and food chemistry
- 1969
Enzymes obtained from an Arthrobacter sp. grown on 2,4-dichlorophenoxyacetic acid catalyzed the conversion of 4-chloroand 3,5-dichlorocatechols to cis,cis-3-chloroand cis,cis-2,4-dichloromuconic…
Degradation of 2,4,6-trichlorophenol by Azotobacter sp. strain GP1
- BiologyApplied and environmental microbiology
- 1991
Induction studies, including treatment of the cells with chloramphenicol prior to TCP or phenol addition, revealed that TCP induced TCP degradation but not phenol degradation and that phenol induced only its own utilization.
Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on 1,2-dioxygenation of catechol.
- Chemistry, BiologyThe Biochemical journal
- 1978
Results from binding studies with substituted catechols demonstrated narrow stereospecificities of pyrocatechase I from pseudomonas sp.
Metabolism of phenol and resorcinol in Trichosporon cutaneum
- Chemistry, BiologyJournal of bacteriology
- 1979
The formation of beta-ketoadipate from phenol, catechol, and resorcinol was shown by a manometric method using antipyrine and also by its isolation and crystallization, and the enzyme catalyzing this reaction was purified some 50-fold.
Metabolism of resorcinylic compounds by bacteria: alternative pathways for resorcinol catabolism in Pseudomonas putida
- Biology, ChemistryJournal of bacteriology
- 1976
Data is presented which shows that one strain of Pseudomonas putida ORC catabolizes resorcinol by a metabolic pathway via hydroxyquinol and ortho oxygenative cleavage to give maleylacetate, but that the other strain (O1) yields mutants that utilize res orcinol.
Catabolism of L-tyrosine in Trichosporon cutaneum
- Biology, ChemistryJournal of bacteriology
- 1979
Evidence is presented that the principal hydroxylation product of protocatechuate was hydroxyquinol, the benzene nucleus of which was cleaved oxidatively to give maleylacetic acid.