Bacterial degradation of monocyclic aromatic amines

Arora, Pankaj

doi:10.3389/fmicb.2015.00820

Cited by 74 publications

(44 citation statements)

References 77 publications

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“…The presence of carboxylic acid moieties in TP304, TP278, TP276, and TP234 clearly indicates the enzymatic cleavage of the aromatic ring in bentazone. This biodegradation reaction, which is common for aromatic compounds (27,28), involves hydroxylation reactions as primary biodegradation step (10,20). This is supported by previous studies showing the formation of 6-OH-, 8-OH-, isopropyl-OH-and di-OHbentazone during bentazone degradation by a methanotrophic enrichment culture enriched from the same rapid sand filter at Sjaelsø waterworks Plant II (20).…”

Section: Degradation Of 6-and 8-oh-bentazone In Filter Sand (Bm1 and supporting

confidence: 70%

Microbial degradation pathways of the herbicide bentazone in filter sand used for drinking water treatment

Hedegaard

Prasse

Albrechtsen

2019

Environ. Sci.: Water Res. Technol.

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Section: Degradation Of 6-and 8-oh-bentazone In Filter Sand (Bm1 and supporting

confidence: 70%

Microbial degradation pathways of the herbicide bentazone in filter sand used for drinking water treatment

Hedegaard

Prasse

Albrechtsen

2019

Environ. Sci.: Water Res. Technol.

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“…PAEM_04659 encoding for the 2-hydroxymuconate (4-oxalocrotonate) tautomerase family protein, related to the metabolism of aromatic compounds, particularly aromatic amines, has no matches within the DSM 500071 T ( Table S7 ), PAO1, and LESB58 genomes, but 100% identity with the multispecies protein [Pseudomonas] (RefSeq: WP_003159697.1), including 13 sequences from the MDR P. aeruginosa strains BL12, BL24, BWHPSA003, BWHPSA017, CF18, X24509, Z61, 3575, BWH050, BWH055, NCMG1179, Pseudomonas knackmussii , and Acinetobacter baumannii , which degrade chloroaromatic compounds [ 35 , 36 ].…”

Section: Resultsmentioning

confidence: 99%

Genomic Features of a Food-Derived Pseudomonas aeruginosa Strain PAEM and Biofilm-Associated Gene Expression under a Marine Bacterial α-Galactosidase

Balabanova

Shkryl

Slepchenko

et al. 2020

IJMS

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The biofilm-producing strains of P. aeruginosa colonize various surfaces, including food products and industry equipment that can cause serious human and animal health problems. The biofilms enable microorganisms to evolve the resistance to antibiotics and disinfectants. Analysis of the P. aeruginosa strain (serotype O6, sequence type 2502), isolated from an environment of meat processing (PAEM) during a ready-to-cook product storage (−20 °C), showed both the mosaic similarity and differences between free-living and clinical strains by their coding DNA sequences. Therefore, a cold shock protein (CspA) has been suggested for consideration of the evolution probability of the cold-adapted P. aeruginosa strains. In addition, the study of the action of cold-active enzymes from marine bacteria against the food-derived pathogen could contribute to the methods for controlling P. aeruginosa biofilms. The genes responsible for bacterial biofilm regulation are predominantly controlled by quorum sensing, and they directly or indirectly participate in the synthesis of extracellular polysaccharides, which are the main element of the intercellular matrix. The levels of expression for 14 biofilm-associated genes of the food-derived P. aeruginosa strain PAEM in the presence of different concentrations of the glycoside hydrolase of family 36, α-galactosidase α-PsGal, from the marine bacterium Pseudoalteromonas sp. KMM 701 were determined. The real-time PCR data clustered these genes into five groups according to the pattern of positive or negative regulation of their expression in response to the action of α-galactosidase. The results revealed a dose-dependent mechanism of the enzymatic effect on the PAEM biofilm synthesis and dispersal genes.

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“…S1). However, related functional enzymes, such as anthranilate 1,2‐dioxygenase and anthranilate hydroxylase (Arora, ), were not identified or upregulated in strain SHE. Anthranilate transformation via the 2‐aminobenzoyl‐CoA pathway in A .…”

Section: Discussionmentioning

confidence: 99%

Unveiling the biotransformation mechanism of indole in a Cupriavidus sp. strain

Liu

et al. 2017

Molecular Microbiology

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Indole, an important signaling molecule as well as a typical N-heterocyclic aromatic pollutant, is widespread in nature. However, the biotransformation mechanisms of indole are still poorly studied. Here, we sought to unlock the genetic determinants of indole biotransformation in strain Cupriavidus sp. SHE based on genomics, proteomics and functional studies. A total of 177 proteins were notably altered (118 up- and 59 downregulated) in cells grown in indole mineral salt medium when compared with that in sodium citrate medium. RT-qPCR and gene knockout assays demonstrated that an indole oxygenase gene cluster was responsible for the indole upstream metabolism. A functional indole oxygenase, termed IndA, was identified in the cluster, and its catalytic efficiency was higher than those of previously reported indole oxidation enzymes. Furthermore, the indole downstream metabolism was found to proceed via the atypical CoA-thioester pathway rather than conventional gentisate and salicylate pathways. This unusual pathway was catalyzed by a conserved 2-aminobenzoyl-CoA gene cluster, among which the 2-aminobenzoyl-CoA ligase initiated anthranilate transformation. This study unveils the genetic determinants of indole biotransformation and will provide new insights into our understanding of indole biodegradation in natural environments and its functional studies.

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Bacterial degradation of monocyclic aromatic amines

Cited by 74 publications

References 77 publications

Microbial degradation pathways of the herbicide bentazone in filter sand used for drinking water treatment

Microbial degradation pathways of the herbicide bentazone in filter sand used for drinking water treatment

Genomic Features of a Food-Derived Pseudomonas aeruginosa Strain PAEM and Biofilm-Associated Gene Expression under a Marine Bacterial α-Galactosidase

Unveiling the biotransformation mechanism of indole in a Cupriavidus sp. strain

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