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Post‐translational modifications in the active site region of methyl‐coenzyme M reductase from methanogenic and methanotrophic archaea
Author(s) -
Kahnt Jörg,
Buchenau Bärbel,
Mahlert Felix,
Krüger Martin,
Shima Seigo,
Thauer Rudolf K.
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.06016.x
Subject(s) - archaea , methanococcus , methanosarcina barkeri , biochemistry , active site , biology , methanogen , crenarchaeota , methanosarcina , cofactor , thermophile , amino acid , stereochemistry , enzyme , bacteria , methanogenesis , chemistry , gene , genetics
Methyl‐coenzyme M reductase (MCR) catalyzes the methane‐forming step in methanogenic archaea. Isoenzyme I from Methanothermobacter marburgensis was 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.