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Substrate diversity and expression of the 2,4,5-trichlorophenoxyacetic acid oxygenase from Burkholderia cepacia AC1100

Article Abstract:

The Burkholderia cepacia AC1100 oxygenase (TftAB) converts 2,4,5-trichlorophenoxyacetic acid to 2,4,5-trichlorophenol and many other chlorinated aromatic phenoxyacetates to their phenolic derivatives. The rate of substrate consumption by TftAB depends upon the degree of substrate chlorination, chlorines position and phenoxy group. There is a mechanistic similarity between TftAB and TfdA of Alcaligenes eutrophus. Escherichia coli and Burkholderia cepacia expresses the promoter cloned upstream of the beta-galactosidase gene and show beta-galactosidase activity.

Author: Chakrabarty, A.M., Ye, Rick W., Danganan, Clyde E., Shankar, Sandeep
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
Observations, Oxidases

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Genes for 2,4,5-trichlorophenoxyacetic acid metabolism in Burkholderia cepacia AC1100: characterization of the tftC and tftD genes and locations of the tft operons on multiple replicons

Article Abstract:

A study was conducted to determine and describe the tftCD gene to characterize the upper portion of the aromatic compound 2,4,5-trichlorophenoxyacetic acid (2,4,5-T) pathway in Burkholderia cepacia. Plasmid-preparative columns were utilized to perform a large-scale purification of cosmids while agarose plugs with intact chromosomal DNA were determined from overnight cultures. Results showed that the genes encoding the 2,4,5-T oxygenase, tftAB, were on replicon IV.

Author: Xun, Luying, Chakrabarty, A.M., Danganan, Clyde E., Hubner, Anette, Hendrickson, William
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Phenols, Phenols (Class of compounds), Aromatic compounds, Trichlorophenoxyacetic acid, 2,4,5-T (Herbicide)

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Purification of hydroxyquinol 1,2-dioxygenase and maleylacetate reductase: the lower pathway of 2,4,5-trichlorophenoxyacetic acid metabolism by Burkholderia cepacia AC1100

Article Abstract:

The enzyme hydroxyquinol 1,2-dioxygenase and maleylacetate reductase have been purified from Escherichia coli cells expressing the Burkholderia cepacia AC1100 tftH gene and tftE gene, respectively. The two enzymes catalyze the formation of 3-oxoadipate from hydroxyquinol. Genetic studies reveal that these enzymes bring about degradation of 2,4,5-trichlorophenoxyacetic acid. Hydroxyquinol 1,2-dioxygenase is a dimeric molecule of 68 kDa.

Author: Chakrabarty, A.M., Daubaras, Dayna L., Saido, Katsuhiko
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
Escherichia coli

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Subjects list: Research, Microbial enzymes
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