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Journal Article

Post-translational modifications in the active site region of methyl-coenzyme M reductase from methanogenic and methanotrophic archaea.

MPS-Authors
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Kahnt,  Joerg
Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Buchenau,  Baerbel
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Mahlert,  Felix
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;

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Thauer,  Rudolf
Emeriti Biochemistry of Anaerobic Microorganisms, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Kahnt, J., Buchenau, B., Mahlert, F., Krueger, M., Shima, S., & Thauer, R. (2007). Post-translational modifications in the active site region of methyl-coenzyme M reductase from methanogenic and methanotrophic archaea. The FEBS Journal, 274, 4913-21. doi:10.1111/j.1742-4658.2007.06016.x.


Cite as: https://hdl.handle.net/21.11116/0000-0007-C6BD-5
Abstract
Methyl-coenzyme M reductase (MCR) catalyzes the methane-forming step in methanogenic archaea. Isoenzyme I from Methanothermobacter marburgensiswas shown to contain a thioxo peptide bond and four methylated amino acids in the active site region. We report here that MCRs from all methanogens investigated contain the thioxo peptide bond, but that the enzymes differ in their post-translational methylations. The MS analysis included MCR I and MCR II from Methanothermobacter marburgensis, MCR I from Methanocaldococcus jannaschii and Methanoculleus thermophilus, and MCR from Methanococcus voltae, Methanopyrus kandleri and Methanosarcina barkeri. Two MCRs isolated from Black Sea mats containing mainly methanotrophic archaea of the ANME-1 cluster were also analyzed.