Capture of a catabolic plasmid that encodes only 2,4-dichlorophenoxyacetic acid:alpha-ketoglutaric acid dioxygenase (TfdA) by genetic complementation

Article Abstract:

The bacterial plasmid pEMT8 contains the tfdA gene that encodes the 2,4-dichlorophenoxyacetic acid (2,4-D):alpha-ketoglutaric acid dioxygenase (TfdA) involved in 2,4-D degradation. The tfdA gene is 94% similar to that of the Burkholderia sp. strain RASC and has somewhat less similarity to that present on the Alcaligenes eutrophus pJP4 plasmid. No genes similar to the tfdB and tfdCDEF are present on pEMT8. The pEMT8 plasmid is captured by genetic complementation of transconjugates of A. eutrophus containing a pJP4 plasmid lacking the tfdA gene and bacteria from the soil.

author: Top, E.M., Maltseva, O.V., Forney, L.J.
Usage, Genetic aspects, Biodegradation, Plasmids, Complementation (Genetics)

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Induction of the D-amino acid oxidase from Trigonopsis variabilis

Article Abstract:

N-carbamoyl-D-alanine is the most effective inducer of the D-amino acid oxidase (D-AO) from the yeast Trigonopsis variabilis. An optimum concentration of 5 mM of the alanine derivative produces a 1.5-fold induction over D-alanine. N-chloroacetyl-D-alpha-aminobutyric acid and N-acetyl-D-tryptophan are also better inducers compared to D-alanine. The pH of the medium has no effect on the induction. Glucose is used as the carbon and energy source and (NH4)2SO4 as the nitrogen source in the medium. Addition of zinc ions produces high levels of D-AO in the cells.

author: Horner, Roy, Wagner, Fritz, Fischer, Lutz
Yeast, Yeast (Food product), Enzyme activation

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Purification and characterization of hydroxyquinol 1,2 dioxygenase from Azotobacter sp. strain GP1

Article Abstract:

The enzyme hydroxyquinol 1,2-dioxygenase was isolated from the soil bacterium Azotobacter sp. strain GP1 grown on 2,4,6 trichlorophenol as the carbon source. This enzyme degrades 2,4,6 trichlorophenol, which is a component of disinfectants and other preservatives. The enzyme had a molecular weight of 58,000 with a sedimentation coefficient of 4.32. It was highly specific for 6-chlorohyroxyquinol and the addition of Fe2+ ions activated the enzyme.

author: Latus, Markus, Seitz, Hans-Jurgen, Eberspacher, Jurgen, Lingens, Franz
Chlorophenols

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subjects list: Research, Oxidases
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