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Volume 160, Issue 12

Anaerobic degradation of aromatic amino acids by the hyperthermophilic archaeon Free

Abstract

was discovered to oxidize completely the aromatic amino acids tyrosine, phenylalanine and tryptophan when Fe(III) oxide was provided as an electron acceptor. This property had not been reported previously for a hyperthermophilic archaeon. It appeared that follows a pathway for phenylalanine and tryptophan degradation similar to that of mesophilic nitrate-reducing bacteria, and EbN1. Phenylacetate, 4-hydroxyphenylacetate and indole-3-acetate were formed during anaerobic degradation of phenylalanine, tyrosine and tryptophan, respectively. Candidate genes for enzymes involved in the anaerobic oxidation of phenylalanine to phenylacetate (phenylalanine transaminase, phenylpyruvate decarboxylase and phenylacetaldehyde : ferredoxin oxidoreductase) were identified in the genome. In addition, transcription of candidate genes for the anaerobic phenylacetate degradation, benzoyl-CoA degradation and glutaryl-CoA degradation pathways was significantly upregulated in microarray and quantitative real-time-PCR studies comparing phenylacetate-grown cells with acetate-grown cells. These results suggested that the general strategies for anaerobic degradation of aromatic amino acids are highly conserved amongst bacteria and archaea living in both mesophilic and hyperthermophilic environments. They also provided insights into the diverse metabolism of species living in hyperthermophilic environments.

  • Received:
  • Accepted:
  • Published Online:
Funding
This study was supported by the:
  • Western New England University and the Office of Science (BER), US Department of Energy (Award DE-SC0006790)
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Anaerobic degradation of aromatic amino acids by the hyperthermophilic archaeon Ferroglobus placidus
Microbiology 160, 2694 (2014); https://doi.org/10.1099/mic.0.083261-0
/content/journal/micro/10.1099/mic.0.083261-0
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