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… 

Purification and Characterization of Hydroxyquinol 1,2-Dioxygenase from Azotobacter sp. Strain GP1

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

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

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

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

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

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

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.

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

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.

Results showed that the hydroxyquinol 1,2-dioxygenase reported here was a novel dioXYgenase that catalyzed both the intradiol and extradiol cleavage of catechol.
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