Publication | Open Access
Protein content and enzyme activities in methanol- and acetate-grown Methanosarcina thermophila
56
Citations
30
References
1990
Year
MethanolMolecular BiologyEnzymatic ModificationBioenergeticsStructure-function Enzyme KineticsAlcohol DehydrogenasesProtein ChemistryAcetate-grown Methanosarcina ThermophilaAldehyde DehydrogenaseBiochemistryFormylmethanofuran DehydrogenaseProtein ContentCellular EnzymologyEnzyme ActivitiesNatural SciencesEnzyme CatalysisBiotechnologyCarbonic AnhydraseMicrobiologyMetabolismMedicineExclusive Spots
The cell extract protein content of acetate- and methanol-grown Methanosarcina thermophila TM-1 was examined by two-dimensional polyacrylamide gel electrophoresis. More than 100 mutually exclusive spots were present in acetate- and methanol-grown cells. Spots corresponding to acetate kinase, phosphotransacetylase, and the five subunits of the carbon monoxide dehydrogenase complex were identified in acetate-grown cells. Activities of formylmethanofuran dehydrogenase, formylmethanofuran:tetrahydromethanopterin formyltransferase, 5,10-methenyltetrahydromethanopterin cyclohydrolase, methylene tetrahydromethanopterin:coenzyme F420 oxidoreductase, formate dehydrogenase, and carbonic anhydrase were examined in acetate- and methanol-grown Methanosarcina thermophila. Levels of formyltransferase in either acetate- or methanol-grown Methanosarcina thermophila were approximately half the levels detected in H2-CO2-grown Methanobacterium thermoautotrophicum. All other enzyme activities were significantly lower in acetate- and methanol-grown Methanosarcina thermophila.
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