CARBONIC-ANHYDRASE ACTIVITY IN ACETATE GROWN METHANOSARCINA-BARKERI
CARBONIC-ANHYDRASE ACTIVITY IN ACETATE GROWN METHANOSARCINA-BARKERI
复制标题
DOI:
10.1007/bf00414428
复制
发表时间:
1989-01-01
影响因子:
2.8
通讯作者:
THAUER, RK
中科院分区:
文献类型:
--
作者:
KARRASCH, M;BOTT, M;THAUER, RK
Cell extracts (27000 .times. g 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 Ki = 0.5 mM), by azide (apparent Ki = 1 mM), and by cyanide (apparent Ki = 0.02 mM). These and other properties indicate that the archaebacterium contains the enzyme carbonic anhydrase (EC 4.2.1.1). Evidences is presented that the protein is probably located in the cytoplasm. Methanol or H2/CO2 grwon 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).