Glutathione-S-transferase activity and metabolism of glutathione conjugates by rhizosphere bacteria

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Abstract

Glutathione-S-transferase (GST) activity was determined in 36 species of rhizosphere bacteria with the substrate 1-chloro-2,4-dinitrobenzene (CDNB) and in 18 strains with the herbicide alachlor. Highest levels of CDNB-GST activity (60 to 222 nmol · h-1 · mg-1) were found in gram-negative bacteria: Enterobacter cloacae, Citrobacter diversus, Klebsiella planticola, Pseudomonas cepacia, Pseudomonas fluorescens, Pseudomonas putida, and Xanthomonas campestris. There was very low CDNB-GST activity in the gram- positive strains. Rapid metabolism of CDNB-glutathione conjugates, attributable to high levels of γ-glutamyltranspeptidase, also occurred in the gram-negative bacteria, especially pseudomonads. Alachlor-GST activity detected in cell extracts and whole-cell suspensions of some strains of the families Enterobacteriaceae and Pseudomonaceae was 50- to 100-fold lower than CDNB-GST activity (0.5 to 2.5 nmol · h-1 · mg-1) and was, for the most part, constitutive. The glutathione-alachlor conjugate was rarely detected. Cysteineglycine and/or cysteine conjugates were the major products of alachlor-GST metabolism. Whole-cell suspensions of certain Pseudomonas spp. dechlorinated from 20 to 75% of 100 μM alachlor in 24 h. Results indicate that rhizosphere bacteria, especially fluorescent pseudomonads, may play an important role in the degradation of xenobiotics such as alachlor via GST- mediated reactions.

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Zablotowicz, R. M., Hoagland, R. E., Locke, M. A., & Hickey, W. J. (1995). Glutathione-S-transferase activity and metabolism of glutathione conjugates by rhizosphere bacteria. Applied and Environmental Microbiology, 61(3), 1054–1060. https://doi.org/10.1128/aem.61.3.1054-1060.1995

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