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The Biosynthesis of Methylated Amino Acids in the Active Site Region of Methyl-coenzyme M Reductase

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Kahnt,  Jörg
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Goubeaud,  Marcel
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Shima,  Seigo
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Grabarse,  Wolfgang
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Thauer,  Rudolf K.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität, D-35032 Marburg, Germany;

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Citation

Selmer, T., Kahnt, J., Goubeaud, M., Shima, S., Grabarse, W., Ermler, U., et al. (2000). The Biosynthesis of Methylated Amino Acids in the Active Site Region of Methyl-coenzyme M Reductase. The Journal of Biological Chemistry, 275(6), 3755-3760. doi:10.1074/jbc.275.6.3755.


Cite as: http://hdl.handle.net/21.11116/0000-0009-4B7E-7
Abstract
The global production of the greenhouse gas methane by methanogenic archaea reaches 1 billion tons per annum. The final reaction releasing methane is catalyzed by the enzyme methyl-coenzyme M reductase. The crystal structure of methyl-coenzyme M reductase from Methanobacterium thermoautotrophicum revealed the presence of five modified amino acids within the alpha-subunit and near the active site region. Four of these modifications were C-, N-, and S-methylations, two of which, 2-(S)-methylglutamine and 5-(S)-methylarginine, have never been encountered before. We have now confirmed these modifications by mass spectrometry of chymotryptic peptides. With methyl-coenzyme M reductase purified from cells grown in the presence of L-[methyl-D3]methionine, it was shown that the methyl groups of the modified amino acids are derived from the methyl group of methionine rather than from methyl-coenzyme M, an intermediate in methane formation. The D3 labeling pattern was found to be qualitatively and quantitatively the same as in the two methyl groups of the methanogenic coenzyme F430, which are known to be introduced via S-adenosylmethionine. From the results, it is concluded that the methyl groups of the modified amino acids in methyl-coenzyme M reductase are biosynthetically introduced by an S-adenosylmethionine-dependent post-translational modification. A mechanism for the methylation of glutamine at C-2 and of arginine at C-5 is discussed.