Involvement of a Selenoprotein in Glycine, Sarcosine, and Betaine Reduction by Eubacterium acidaminophilum

Freudenberg, W.; Hormann, K.; Rieth, M.; Andreesen, Jan R.

doi:10.1007/978-3-642-74421-1_5

Cited by 4 publications

(2 citation statements)

References 17 publications

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“…The close relationship of the dihydrolipoamide dehydrogenase of E. acidaminophilum to thioredoxin reductase as uncovered in this study correlates with its close association to the cytoplasmic membrane and with the selenoprotein being part of the glycine reductase complex (12,13). Sarcosine reductase and betaine reductase are separate enzymes from glycine reductase; however, these reductases might share the dihydrolipoamide dehydrogenase and the selenoprotein PA as common constituents (22 (10).…”

Section: Discussionsupporting

confidence: 60%

Purification of NADPH-dependent electron-transferring flavoproteins and N-terminal protein sequence data of dihydrolipoamide dehydrogenases from anaerobic, glycine-utilizing bacteria

et al. 1990

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Three electron-transferring flavoproteins were purified to homogeneity from anaerobic, amino acid-utilizing bacteria (bacterium W6, Clostridium sporogenes, and Clostridium sticklandii), characterized, and compared with the dihydrolipoamide dehydrogenase of Eubacterium acidaminophilum. All the proteins were found to be dimers consisting of two identical subunits with a subunit Mr of about 35,000 and to contain about 1 mol of flavin adenine dinucleotide per subunit. Spect.ra of the oxidized proteins exhibited characteristic absorption of flavoproteins, and the reduced proteins showed an A580 indicating a neutral'semiquinone. Many artificial electron acceptors, including methyl viologen, could be used with NADPH as the electron donor but not with NADH. Unlike the enzyme'of E. acidaminophilum, which exhibited by itself a dihydrolipoamide dehydrogenase activity (W. Freudenberg, D. Dietrichs, H. Lebertz, and J. R. Andreesen, J. Bacteriol. 171:1346Bacteriol. 171: -1354Bacteriol. 171: , 1989, the electron-transferring flavoprotein purified from bacterium W6 reacted with lipoamide only under certain assay conditions, whereas the proteins of C. sporogenes and C. sticklandii exhibited no dihydrolipoamide dehydrogenase activity. The three homogeneous electron-transferring flavoproteins were very similar in their structural and biochemical properties to the dihydrolipoamide dehydrogenase of E. acidaminophilum and exhibited cross-reaction with antibodies raised against the latter enzyme. N-terminal sequence analysis demonstrated a high degree of homology between the dihydrolipoamide dehydrogenase of E. acidaminophilum and the electron-transferring fiavoprotein of C. sporogenes to the thioredoxin reductase of Escherichia coli. Unlike these proteins, the dihydrolipoamide dehydrogenases purified from' the anaerobic, glycine-utilizing bacteria Peptostreptococcus glycinophilus, Clostridium cylindrosporum, and C. sporogenes exhibited a high homology to dihydrolipoamide dehydrogenases known from other organisms.

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Section: Discussionsupporting

confidence: 60%

Purification of NADPH-dependent electron-transferring flavoproteins and N-terminal protein sequence data of dihydrolipoamide dehydrogenases from anaerobic, glycine-utilizing bacteria

et al. 1990

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“…The glycine betaine (GrdH) pathway was detected at relatively low levels, which may be attributed to its requirement for the trace element, selenium, for enzyme activity ( Freudenberg et al , 1989 ). Clinical studies found a link between low plasma concentrations of selenium and CVD, while selenium supplementation trials did not improve outcomes ( Flores-Mateo et al ., 2006 ; Fairweather-Tait et al , 2011 ); potentially indicating a selenium requirement by a CVD-inducing GrdH containing bacterial community ( Freudenberg et al , 1989 ). It is also likely that low abundance of GrdH in the gut metagenome was due to GBTs importance as a compatible solute.…”

Section: Resultsmentioning

confidence: 99%

Metagenomic data-mining reveals contrasting microbial populations responsible for trimethylamine formation in human gut and marine ecosystems

et al. 2016

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Existing metagenome datasets from many different environments contain untapped potential for understanding metabolic pathways and their biological impact. Our interest lies in the formation of trimethylamine (TMA), a key metabolite in both human health and climate change. Here, we focus on bacterial degradation pathways for choline, carnitine, glycine betaine and trimethylamine N-oxide (TMAO) to TMA in human gut and marine metagenomes. We found the TMAO reductase pathway was the most prevalent pathway in both environments. Proteobacteria were found to contribute the majority of the TMAO reductase pathway sequences, except in the stressed gut, where Actinobacteria dominated. Interestingly, in the human gut metagenomes, a high proportion of the Proteobacteria hits were accounted for by the genera Klebsiella and Escherichia. Furthermore Klebsiella and Escherichia harboured three of the four potential TMA-production pathways (choline, carnitine and TMAO), suggesting they have a key role in TMA cycling in the human gut. In addition to the intensive TMAO–TMA cycling in the marine environment, our data suggest that carnitine-to-TMA transformation plays an overlooked role in aerobic marine surface waters, whereas choline-to-TMA transformation is important in anaerobic marine sediments. Our study provides new insights into the potential key microbes and metabolic pathways for TMA formation in two contrasting environments.

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Reductive cleavage of sarcosine and betaine by Eubacterium acidaminophilum via enzyme systems different from glycine reductase

Hormann

Andreesen

1989

Arch. Microbiol.

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Involvement of a Selenoprotein in Glycine, Sarcosine, and Betaine Reduction by Eubacterium acidaminophilum

Cited by 4 publications

References 17 publications

Purification of NADPH-dependent electron-transferring flavoproteins and N-terminal protein sequence data of dihydrolipoamide dehydrogenases from anaerobic, glycine-utilizing bacteria

Purification of NADPH-dependent electron-transferring flavoproteins and N-terminal protein sequence data of dihydrolipoamide dehydrogenases from anaerobic, glycine-utilizing bacteria

Metagenomic data-mining reveals contrasting microbial populations responsible for trimethylamine formation in human gut and marine ecosystems

Reductive cleavage of sarcosine and betaine by Eubacterium acidaminophilum via enzyme systems different from glycine reductase

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