Proteomics

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Comparative proteomics of Eubacterium maltosivorans: Functional identification of trimethylamine methyltransferases and bacterial microcompartments in a human intestinal bacterium


ABSTRACT: This study was conducted in order to explore proteins involved in quaternary amines degradation and microcompartments formation of E. maltosivorans.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Eubacterium Maltosivorans

SUBMITTER: Sjef Boeren  

LAB HEAD: Sjef Boeren

PROVIDER: PXD028574 | Pride | 2022-08-12

REPOSITORIES: Pride

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Publications

Comparative genomics and proteomics of Eubacterium maltosivorans: functional identification of trimethylamine methyltransferases and bacterial microcompartments in a human intestinal bacterium with a versatile lifestyle.

Feng Yuan Y   Bui Thi Phuong Nam TPN   Stams Alfons J M AJM   Boeren Sjef S   Sánchez-Andrea Irene I   de Vos Willem M WM  

Environmental microbiology 20220102 1


Eubacterium maltosivorans YI<sup>T</sup> is a human intestinal isolate capable of acetogenic, propionogenic and butyrogenic growth. Its 4.3-Mb genome sequence contains coding sequences for 4227 proteins, including 41 different methyltransferases. Comparative proteomics of strain YI<sup>T</sup> showed the Wood-Ljungdahl pathway proteins to be actively produced during homoacetogenic growth on H<sub>2</sub> and CO<sub>2</sub> while butyrogenic growth on a mixture of lactate and acetate significantl  ...[more]

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