title: Function of methylcobalamin: coenzyme M methyltransferase isoenzyme II in Methanosarcina barkeri.
abstract: Methanosarcina barkeri was recently shown to contain two cytoplasmic isoenzymes of methylcobalamin: coenzyme M methyltransferase (methyltransferase 2). Isoenzyme I predominated in methanol-grown cells and isoenzyme II in acetate-grown cells. It was therefore suggested that isoenzyme I functions in methanogenesis from methanol and isoenzyme II in methanogenesis from acetate. We report here that cells of M. barkeri grown on trimethylamine, H2/CO2, or acetate contain mainly isoenzyme II. These cells were found to have in common that they can catalyze the formation of methane from trimethylamine and H2, whereas only acetate-grown cells can mediate the formation of methane from acetate. Methanol-grown cells, which contained only low concentrations of isoenzyme II, were unable to mediate the formation of methane from both trimethylamine and acetate. These and other results suggest that isoenzyme II (i) is employed for methane formation from trimethylamine rather than from acetate, (ii) is constitutively expressed rather than trimethylamine-induced, and (iii) is repressed by methanol. The constitutive expression of isoenzyme II in acetate-grown M. barkeri can explain its presence in these cells. The N-terminal amino acid sequences of isoenzyme I and isoenzyme II were analyzed and found to be only 55% similar.
authors.affiliation: Laboratorium für Mikrobiologie des Fachbereichs Biologie der Philipps-Universität Marburg, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Yeliseev
authors.forename: P
authors.initials: P
authors.lastname: Gärtner
authors.forename: U
authors.initials: U
authors.lastname: Harms
authors.forename: D
authors.initials: D
authors.lastname: Linder
authors.forename: R K
authors.initials: RK
authors.lastname: Thauer
mesh_terms: D000085:Acetates / Q000378:metabolism; D000595:Amino Acid Sequence; D019843:Archaeal Proteins; D002245:Carbon Dioxide / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D019605:Euryarchaeota / Q000201:enzymology; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008697:Methane / Q000378:metabolism; D000432:Methanol / Q000378:metabolism; D017021:Methanosarcina barkeri / Q000201:enzymology*; D008744:Methylamines / Q000378:metabolism; D008780:Methyltransferases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D014805:Vitamin B 12 / Q000031:analogs & derivatives* / Q000378:metabolism
chemical_list: D000085:Acetates; D019843:Archaeal Proteins; D007527:Isoenzymes; D008744:Methylamines; D002245:Carbon Dioxide; C019476:mecobalamin; D008780:Methyltransferases; C023894:methylcobalamin-coenzyme M methyltransferase; C023336:trimethylamine; D008697:Methane; D014805:Vitamin B 12; D000432:Methanol