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A Novel Acyl-CoA Beta-Transaminase Characterized from a Metagenome
BACKGROUND: Bacteria are key components in all ecosystems. However, our knowledge of bacterial metabolism is based solely on the study of cultivated organisms which represent just a tiny fraction of microbial diversity. To access new enzymatic reactions and new or alternative pathways, we investigat...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3149608/ https://www.ncbi.nlm.nih.gov/pubmed/21826218 http://dx.doi.org/10.1371/journal.pone.0022918 |
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author | Perret, Alain Lechaplais, Christophe Tricot, Sabine Perchat, Nadia Vergne, Carine Pellé, Christine Bastard, Karine Kreimeyer, Annett Vallenet, David Zaparucha, Anne Weissenbach, Jean Salanoubat, Marcel |
author_facet | Perret, Alain Lechaplais, Christophe Tricot, Sabine Perchat, Nadia Vergne, Carine Pellé, Christine Bastard, Karine Kreimeyer, Annett Vallenet, David Zaparucha, Anne Weissenbach, Jean Salanoubat, Marcel |
author_sort | Perret, Alain |
collection | PubMed |
description | BACKGROUND: Bacteria are key components in all ecosystems. However, our knowledge of bacterial metabolism is based solely on the study of cultivated organisms which represent just a tiny fraction of microbial diversity. To access new enzymatic reactions and new or alternative pathways, we investigated bacterial metabolism through analyses of uncultivated bacterial consortia. METHODOLOGY/PRINCIPAL FINDINGS: We applied the gene context approach to assembled sequences of the metagenome of the anaerobic digester of a municipal wastewater treatment plant, and identified a new gene which may participate in an alternative pathway of lysine fermentation. CONCLUSIONS: We characterized a novel, unique aminotransferase that acts exclusively on Coenzyme A (CoA) esters, and proposed a variant route for lysine fermentation. Results suggest that most of the lysine fermenting organisms use this new pathway in the digester. Its presence in organisms representative of two distinct bacterial divisions indicate that it may also be present in other organisms. |
format | Online Article Text |
id | pubmed-3149608 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-31496082011-08-08 A Novel Acyl-CoA Beta-Transaminase Characterized from a Metagenome Perret, Alain Lechaplais, Christophe Tricot, Sabine Perchat, Nadia Vergne, Carine Pellé, Christine Bastard, Karine Kreimeyer, Annett Vallenet, David Zaparucha, Anne Weissenbach, Jean Salanoubat, Marcel PLoS One Research Article BACKGROUND: Bacteria are key components in all ecosystems. However, our knowledge of bacterial metabolism is based solely on the study of cultivated organisms which represent just a tiny fraction of microbial diversity. To access new enzymatic reactions and new or alternative pathways, we investigated bacterial metabolism through analyses of uncultivated bacterial consortia. METHODOLOGY/PRINCIPAL FINDINGS: We applied the gene context approach to assembled sequences of the metagenome of the anaerobic digester of a municipal wastewater treatment plant, and identified a new gene which may participate in an alternative pathway of lysine fermentation. CONCLUSIONS: We characterized a novel, unique aminotransferase that acts exclusively on Coenzyme A (CoA) esters, and proposed a variant route for lysine fermentation. Results suggest that most of the lysine fermenting organisms use this new pathway in the digester. Its presence in organisms representative of two distinct bacterial divisions indicate that it may also be present in other organisms. Public Library of Science 2011-08-03 /pmc/articles/PMC3149608/ /pubmed/21826218 http://dx.doi.org/10.1371/journal.pone.0022918 Text en Perret et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Perret, Alain Lechaplais, Christophe Tricot, Sabine Perchat, Nadia Vergne, Carine Pellé, Christine Bastard, Karine Kreimeyer, Annett Vallenet, David Zaparucha, Anne Weissenbach, Jean Salanoubat, Marcel A Novel Acyl-CoA Beta-Transaminase Characterized from a Metagenome |
title | A Novel Acyl-CoA Beta-Transaminase Characterized from a Metagenome |
title_full | A Novel Acyl-CoA Beta-Transaminase Characterized from a Metagenome |
title_fullStr | A Novel Acyl-CoA Beta-Transaminase Characterized from a Metagenome |
title_full_unstemmed | A Novel Acyl-CoA Beta-Transaminase Characterized from a Metagenome |
title_short | A Novel Acyl-CoA Beta-Transaminase Characterized from a Metagenome |
title_sort | novel acyl-coa beta-transaminase characterized from a metagenome |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3149608/ https://www.ncbi.nlm.nih.gov/pubmed/21826218 http://dx.doi.org/10.1371/journal.pone.0022918 |
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