Ontology highlight
ABSTRACT:
PROVIDER: PRJNA944376 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Some acetogenic bacteria, such as Eubacterium limosum, have the native ability to consume liquid C1 feedstocks, such as formate and methanol, as the sole substrate for growth. Due to high energy efficiency, and compatibility with existing infrastructure, this has sparked interest in the biotechnology industry. Previously, we reported limitations of this metabolism in batch fermentation. Here we undertook chemostat differential analysis to highlight key features and bottlenecks of metabolism. Our work serves as a reference dataset to advance understanding of liquid C1 metabolism in acetogens.
2023-04-13 | PXD040283 | Pride
Project description:To understand transcriptional regulation of Eubacterium limosum KIST612 across different carbon/energy/electron sources, RNAseq analysis was carried out over different substrate conditions (glucose, CO, H2/CO2).
2020-04-25 | GSE149269 | GEO
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.
2020-06-19 | PXD013961 | Pride
Project description: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.
2019-07-25 | PXD013806 | Pride
Project description:Eubacterium limosum ATCC 8486 makes acetate and butyrate from various substrates and is found in the human intestine. The proteome of gamma-butyrobetaine -grown Eubacterium limosum was obtained in order to identify enzymes required for growth on gamma-butyrobetaine, in particular to identify components that are unique to growth on gamma-butyrobetaine in comparison to other substrates for acetogenesis, such as lactic acid, L-carnitine, or proline betaine. Gamma-butyrobetaine is converted to trimethylamine (TMA) by certain members of the gut microbiome. Subsequent liver metabolism of TMA is now tied to progression of cardiovascular disease. Demethylation of gamma-butyrobetaine is observed during growth of Eubacterium limosum on this substrate, and does not produce TMA. Gamma-butyrobetaine demethylation by organisms like Eubacterium limosum could lessen TMA production in the gut, thereby lessening the propensity towards atherosclerosis caused by metabolism of TMA in the body. This proteome led to discovery of gamma-butyrobetaine:tetrahydrofolate methyltransferase system. The key gamma-butyrobetaine demethylating enzyme is a member of the widespread TMA methyltransferase protein superfamily.
2021-11-04 | PXD020152 | Pride
Project description:Eubacterium limosum 32_A2 genome sequencing
| PRJNA311425 | ENA