Methanol metabolism in the acetogenic bacterium <i>Acetobacterium woodii</i>

Kremp, Florian; Poehlein, Anja; Daniel, Rolf; Müller, Volker

doi:10.1111/1462-2920.14356

Cited by 73 publications

(110 citation statements)

References 72 publications

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“…The utilization of MtqA, MtqC, and RamQ in methylating THF with distinct quaternary amines is reflected in the genomic context of these genes. For example, both ramQ and mtqA are located near a number of genes encoding enzymes involved in the oxidation of methyl-THF (42), an obligate pathway for methylotrophic acetogenesis (49). The methyltransferases are found in other parts of the genome.…”

Section: Discussionmentioning

confidence: 99%

MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase

Kountz

Behrman

Zhang

et al. 2020

Journal of Biological Chemistry

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The trimethylamine methyltransferase MttB is the first described member of a superfamily comprising thousands of microbial proteins. Most members of the MttB superfamily are encoded by genes that lack the codon for pyrrolysine characteristic of trimethylamine methyltransferases, raising questions about the activities of these proteins. The superfamily member MtcB is found in the human intestinal isolate Eubacterium limosum ATCC 8486, an acetogen that can grow by demethylation of L-carnitine. Here, we demonstrate that MtcB catalyzes L-carnitine demethylation. When growing on L-carnitine, E. limosum excreted the unusual biological product norcarnitine as well as acetate, butyrate, and caproate. Cellular extracts of E. limosum grown on L-carnitine, but not lactate, methylated cob(I)alamin or tetrahydrofolate using L-carnitine as methyl donor. MtcB, along with the corrinoid protein MtqC, and the methyl-corrinoid:tetrahydrofolate methyltransferase MtqA were much more abundant in E. limosum cells grown on L-carnitine than on lactate. Recombinant MtcB methylates either cob(I)alamin or Co(I)-MtqC in the presence of L-carnitine, and to a much lesser extent, γ-butyrobetaine. Other quaternary amines were not substrates. Recombinant MtcB, MtqC, and MtqA methylated tetrahydrofolate via L-carnitine, forming a key intermediate in the acetogenic Wood-Ljungdahl pathway. To our knowledge MtcB methylation of cobalamin or Co(I)-MtqC represents the first described mechanism of biological L-carnitine demethylation. The conversion of L-carnitine and its derivative γ-butyrobetaine to trimethylamine by the gut microbiome has been linked to cardiovascular disease. The activities of MtcB and related proteins in E. limosum might demethylate proatherogenic quaternary amines and contribute to the perceived health benefits of this human gut symbiont.

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Section: Discussionmentioning

confidence: 99%

MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase

Kountz

Behrman

Zhang

et al. 2020

Journal of Biological Chemistry

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“…The two single-carbon units are then combined with CoA to produce acetyl-CoA via acetyl-CoA synthase. During methylotrophic acetogenesis, the same enzymes composing the methyl branch operate in the reverse direction, as methyl-THF is generated directly from the substrate (46). Methyl-THF must then be oxidized to generate the reducing power to make acetyl-CoA from methyl-THF and CO 2 .…”

Section: Discussionmentioning

confidence: 99%

MtpB, a member of the MttB superfamily from the human intestinal acetogen Eubacterium limosum, catalyzes proline betaine demethylation

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Behrman

Zhang

et al. 2019

Journal of Biological Chemistry

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“…Figure summarizes the metabolism of GB in A. woodii . The methylene‐tetrahydrofolate reductase is not electron bifurcating (Bertsch et al ., ; Kremp et al ., ) and the electron bifurcating hydrogenase as well as the Rnf complex are required to reduce ferredoxin with NADH and H 2 as reductant according to

\begin{matrix} centertrue \\ {normalH}_{2} + 0.5 {NAD}^{+} + 0.5 Fd \to 1.5 {normalH}^{+} + 0.5 NADH + 0.5 {Fd}^{2 -} \end{matrix}

\begin{matrix} centertrue \\ 2.5 NADH + 5 {Na}_{out}^{+} + 2.5 Fd \to 2.5 {NAD}^{+} + 2.5 {normalH}^{+} + 5 {Na}_{in}^{+} + 2.5 {Fd}^{2 -} . \end{matrix}

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Section: Discussionmentioning

confidence: 99%

Glycine betaine metabolism in the acetogenic bacterium Acetobacterium woodii

Lechtenfeld

Heine

Sameith

et al. 2018

Environmental Microbiology

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The quarternary, trimethylated amine glycine betaine (GB) is widespread in nature but its fate under anoxic conditions remains elusive. It can be used by some acetogenic bacteria as carbon and energy source but the pathway of GB metabolism has not been elucidated. We have identified a gene cluster involved in GB metabolism and studied acetogenesis from GB in the model acetogen Acetobacterium woodii. GB is taken up by a secondary active, Na coupled transporter of the betaine-choline-carnitine (BCC) family. GB is demethylated to dimethylglycine, the end product of the reaction, by a methyltransferase system. Further conversion of the methyl group requires CO as well as Na indicating that GB metabolism involves the Wood-Ljungdahl pathway. These studies culminate in a model for the path of carbon and electrons during acetogenensis from GB and a model for the bioenergetics of acetogenesis from GB.

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Methanol metabolism in the acetogenic bacterium Acetobacterium woodii

Cited by 73 publications

References 72 publications

MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase

MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase

MtpB, a member of the MttB superfamily from the human intestinal acetogen Eubacterium limosum, catalyzes proline betaine demethylation

Glycine betaine metabolism in the acetogenic bacterium Acetobacterium woodii

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