Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: Unusual amino acid modification, conservation and adaptation

Journal of Molecular Biology

Volumn 303, Issue 2, 2000, Pages 329-344

  Grabarse, Wolfgang ^a,b   Mahlert, Felix ^b   Shima, Seigo ^b   Thauer, Rudolf K ^b   Ermler, Ulrich ^a  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

Author keywords

Amino acid methylation; Hyperthermophilicity; Methanogenesis; Methyl coenzyme M reductase; Thiopeptide

Indexed keywords

AMINO ACID DERIVATIVE; METHANE; OXIDOREDUCTASE;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL MODIFICATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; GENETIC CONSERVATION; METHANOBACTERIUM; METHANOGENESIS; METHYLATION; MOLECULAR EVOLUTION; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; TEMPERATURE ACCLIMATIZATION;

ARCHAEA; METHANOBACTERIUM; METHANOPYRUS KANDLERI; METHANOSARCINA BARKERI; METHANOTHERMOBACTER THERMAUTOTROPHICUS;

EID: 0034692923     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4136     Document Type: Article

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