K+-ATPase from Rhizobium sp. UMKL 20


An ATPase whose activity was stimulated by K+ was identified in Rhizobium sp. UMKL 20. The synthesis of the ATPase was repressed by high levels of K+. The enzyme had a pH optimum of about 8.0. It was highly specific for cations and only K+ appeared to be able to stimulate the enzyme. In terms of divalent cation specificity, both Mn2+ and Mg2+ stimulated K+-ATPase activity. ATP was the only nucleotide capable of supporting substantial activity. Vanadate was an inhibitor of the enzyme.

DOI: 10.1007/BF00491910

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@article{Lim2004KATPaseFR, title={K+-ATPase from Rhizobium sp. UMKL 20}, author={Suk Tae Lim}, journal={Archives of Microbiology}, year={2004}, volume={142}, pages={393-396} }