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

Kahnt, J., Buchenau, B., Mahlert, F., Krueger, M., Shima, S., & Thauer, R. K. (2007). Post-translational modifications in the active site region of methyl-coenzyme M reductase from methanogenic and methanotrophic archaea. The FEBS Journal, 274, 4913-4921. doi:10.1111/j.1742-4658.2007.06016.x.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-C6BD-5 Version Permalink: https://hdl.handle.net/21.11116/0000-000F-B4F4-2
Genre: Journal Article

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https://doi.org/10.1111/j.1742-4658.2007.06016.x (Publisher version)
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 Creators:
Kahnt, Joerg1, 2, Author           
Buchenau, Baerbel2, Author           
Mahlert, Felix2, Author           
Krueger, Martin, Author
Shima, Seigo2, 3, Author           
Thauer, Rudolf K.2, Author                 
Affiliations:
1Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266280              
2Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266311              
3Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              

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 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.

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Language(s): eng - English
 Dates: 2007-08-24
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 328877
DOI: 10.1111/j.1742-4658.2007.06016.x
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Title: The FEBS Journal
  Other : The Federation of European Biochemical Societies Journal
Source Genre: Journal
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Publ. Info: Wiley-Blackwell
Pages: - Volume / Issue: 274 Sequence Number: - Start / End Page: 4913 - 4921 Identifier: ISSN: 1742-464X
CoNE: https://pure.mpg.de/cone/journals/resource/954925398485