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Phenylobacterium immobile gen. nov., sp. nov., a Gram-Negative Bacterium That Degrades the Herbicide Chloridazon

Bacteria which utilize the xenobiotic compounds chloridazon, antipyrin, and pyramidon as sole carbon sources were isolated from various soil samples and characterized as a new genus, Phenylobacterium, with a single species,phenylobacteria immobile, which is a serologically uniform group of organisms, which are harmless to rats and rabbits.
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Bacterial dehalogenases: biochemistry, genetics, and biotechnological applications

This review is a survey of bacterial dehalogenases that catalyze the cleavage of halogen substituents from haloaromatics, haloalkanes, haloalcohols, and haloalkanoic acids. Concerning the enzymatic…
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The metabolism of caffeine by a Pseudomonas putida strain.

A pathway of caffeine degradation is proposed and formaldehyde has been demonstrated to be the product of oxidative N-demethylation mediated by an inducible demethylase.
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2-Haloacid dehalogenase from a 4-chlorobenzoate-degrading Pseudomonas spec. CBS 3.

Pseudomonas spec. CBS 3 contains a 2-haloacid dehalogenase induced by chloroacetate. The enzyme was purified about 25-fold to electrophoretic homogeneity by ammonium sulfate fractionation,…
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Purification and characterization of 6-chlorohydroxyquinol 1,2-dioxygenase from Streptomyces rochei 303: comparison with an analogous enzyme from Azotobacter sp. strain GP1

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 and appeared to be a dimer of two identical 31-kDa subunits.
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Degradation of 2,4,6-trichlorophenol by Azotobacter sp. strain GP1

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.
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Purification and some properties of 2-halobenzoate 1,2-dioxygenase, a two-component enzyme system from Pseudomonas cepacia 2CBS

The two components of the inducible 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS were purified to homogeneity and exhibited a very broad substrate specificity, but benzoate analogs with electron-withdrawing substituents at the ortho position were transformed preferentially.
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Flavonol 2,4-dioxygenase from Aspergillus niger DSM 821, a type 2 CuII-containing glycoprotein.

The EPR spectrum of flavonol 2,4-dioxygenase (as isolated) showed the characteristic parameters of a nonblue type 2 CuII protein, and metal chelating agents strongly inhibited the enzymatic activity, but inactivation was not accompanied by loss of copper.
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Cloning, nucleotide sequence, and expression of the plasmid-encoded genes for the two-component 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS

Functional NADH:acceptor reductase and oxygenase components of 2-halobenzoate 1,2-dioxygenase were enriched from recombinant Pseudomonas clones.
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Quinaldine 4-oxidase from Arthrobacter sp. Rü61a, a versatile procaryotic molybdenum-containing hydroxylase active towards N-containing heterocyclic compounds and aromatic aldehydes.

Quinaldine 4-oxidase is unusual in its substrate and electron-acceptor specificity, and catalyzes the oxidation of the aromatic aldehydes, although being progressively inhibited.
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