Abstract
Cell extracts (27000xg supernatant) of acetate grown Methanosarcina barkeri were found to have carbonic anhydrase activity (0.41 U/mg protein), which was lost upon heating or incubation with proteinase K. The activity was inhibited by Diamox (apparent K i=0.5 mM), by azide (apparent K i=1 mM), and by cyanide (apparent K i=0.02 mM). These and other properties indicate that the archaebacterium contains the enzyme carbonic anhydrase (EC 4.2.1.1). Evidence is presented that the protein is probably located in the cytoplasm. Methanol or H2/CO2 grown cells of M. barkeri showed no or only very little carbonic anhydrase activity. After transfer of these cells to acetate medium the activity was “induced” suggesting a function of this enzyme in acetate fermentation to CO2 and CH4. Interestingly, Desulfobacter postgatei and Desulfotomaculum acetoxidans, which oxidize acetate to 2 CO2 with sulfate as electron acceptor, were also found to exhibit carbonic anhydrase activity (0.2 U/mg protein).
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Karrasch, M., Bott, M. & Thauer, R.K. Carbonic anhydrase activity in acetate grown Methanosarcina barkeri . Arch. Microbiol. 151, 137–142 (1989). https://doi.org/10.1007/BF00414428
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DOI: https://doi.org/10.1007/BF00414428