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Journal Article

Tetramethylammonium : coenzyme M methyltransferase system from Methanococcoides sp.

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Liesack,  W       
Department-Independent Research Group Methanotrophic Bacteria, and Environmental Genomics/Transcriptomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Thauer,  R.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Asakawa, S., Sauer, K., Liesack, W., & Thauer, R. (1998). Tetramethylammonium: coenzyme M methyltransferase system from Methanococcoides sp. ARCHIVES OF MICROBIOLOGY, 170(4), 220-226. doi:10.1007/s002030050636.


Cite as: https://hdl.handle.net/21.11116/0000-000D-6B19-0
Abstract
A methanogen (strain NaT1) that belongs to the family of Methanosarcinaceae and that can grow on tetramethylammonium as the sole energy source has recently been isolated. We report here that cell extracts of the archaeon catalyze the formation of methyl-coenzyme M from coenzyme M and tetramethylammonium The activity was dependent on the presence of Ti(III) citrate and ATP, and was rapidly lost under oxic conditions. Anoxic chromatography on DEAE-Sepharose revealed that two fractions, fractions 3 and 4, were required for activity. A 50-kDa protein that together with fraction 3 catalyzed methyl-coenzyme M formation from tetramethylammonium and coenzyme M was purified from fraction 4. From fraction 3, a 22-kDa corrinoid protein and a 40-kDa protein exhibiting methylcobalamin:coenzyme M methyltransferase (MT2) activity were purified. The N-terminal amino acid sequences of these purified proteins were determined. The 40-kDa protein showed sequence similarity to MT2 isoenzymes from Methanosarcina barkeri. Cell extract of strain NaT1 grown on trimethylamine rather than on tetramethylammonium did not exhibit tetramethylammonium:coenzyme M methyltransferase activity. The strain was identified as belonging to the genus of Methanococcoides, its closest relative being Methanococcoides methylutens.