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Proteome of lactate grown Eubacterium limosum ATCC 8486

ABSTRACT: Eubacterium limosum ATCC 8486 makes acetate and butyrate from various substrates and is found in the human intestine. The proteome of lactate-grown Eubacterium limosum was obtained in order to identify enzymes required for growth on this substrate, in particular to identify components that are unique to growth on lactate in comparison to other substrates for acetogenesis.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Bacteria Eubacterium Limosum

SUBMITTER: Joseph Krzycki

LAB HEAD: Joseph Adrian Krzycki

PROVIDER: PXD013806 | Pride | 2019-07-25

REPOSITORIES: Pride

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			Action	DRS
	31823_Sample2_JK_8F_1.raw	Raw
	31823_Sample2_JK_8F_2.raw	Raw
	31823_Sample2_JK_8F_3.raw	Raw
	31823_Sample2_JK_8F_4.raw	Raw
	31823_Sample2_JK_8F_5.raw	Raw

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Project description:Eubacterium limosum ATCC 8486 makes acetate and butyrate from various substrates and is found in the human intestine. The proteome of L-carnitine-grown Eubacterium limosum was obtained in order to identify enzymes required for growth on L-carnitine, in particular to identify components that are unique to growth on L-carnitine in comparison to other substrates for acetogenesis, such as lactic acid. L-carnitine and derviatives are converted to trimethylamine (TMA) by certain members of the gut microbiome, metabolism of TMA is now tied to progression of cardiovascular disease. Demethylation of carnitine is observed during growth of Eubacterium limosum on this substrate, and does not produce TMA. Carnitine demethylation by organisms like Eubacterium limosum could lessen TMA production in the gut, thereby lessening the propensity towards atherorsclerosis caused by metabolism of TMA in the body. The carnitine proteome led to the description of a carnitine:tetrahydrofolate methyltransferase system. The key carnitine demethylating enzyme is a member of the widespread TMA methyltransferase protein superfamily.

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