A novel acyl-CoA beta-transaminase characterized from a metagenome.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 21826218.
- Also identified by DOI 10.1371/journal.pone.0022918 and PMC identifier 3149608.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
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.
Medical subject headings
- Anaerobiosis
- Coenzyme A
- Coenzyme A/metabolism
- Fermentation
- Lysine
- Lysine/metabolism
- Metagenome
- Molecular Structure
- Signal Transduction
- Transaminases
- Transaminases/genetics
- Transaminases/metabolism