Abstract
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.
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Abbreviations
- K+-ATPase:
-
K+-stimulated ATPase
- DCCD:
-
N,N1-dichlorohexylcarbodiimide
- HEPES:
-
N-2-hydroxyethylpiperazine-N1-2-ethanesulfonic acid
- PMSF:
-
phenylmethylsulfonyl fluoride
- TCA:
-
trichloroacetic aci
References
Abrams A, Smith JB (1974) Bacterial membrane ATPase. In: Bayer PD (ed) The enzymes, 3rd ed, vol 10., Academic Press. New York
Bakker EP, Harold RM (1980) Energy coupling to potassium transport in Streptococcus faecalis: interplay of ATP and the proton motive force. J Biol Chem 255: 433–440
Beauge L (1979) Vanadate-K+ interactions in the inhibition of (Na+, K+) ATPase. In: Skan JC, Norby JG (eds) Na+−K+ ATPase: Structures and kinetics. Academic Press, New York
Epstein W, Whitelaw, V., Hesse J (1978) A K+ transport ATPase in E. coli. J Biol Chem 253:6666–6668
Epstein W, Laimins L (1980) Potassium transport in E. coli: diverse systems with common control by osmotic force. Trends Biochem Sci 5:21–23
Heefner DL, Kobayashi H, Harold FM (1980) ATP-linked sodium transport in Streptococcus faecalis. J Biol Chem 255:11403–11407
Hugentobler G, Heid I, Solioz M (1983) Purification of a putative K+-ATPase from Streptococcus faecalis. J Biol Chem 258:7611–7617
Kobayashi H (1982) Second system for potassium transport in Streptococcus faecalis. J Bacteriol 150:506–511
Laimins LA, Rhoads DB, Epstein W (1981) Osmotic control of kdp operon expression in E. coli. Proc Natl Acad Sci USA 78:464–468
Lim ST, Shanmugam KT (1978) Regulation of hydrogen utilization in Rhizobium japonicum by cyclic AMP. Biochem Biophys Acta 584:479–492
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin-phenol reagent. J Biol Chem 193:265–272
Measures JC (1975) Role of amino acids in osmoregulation of nonhalophilic bacteria. Nature (Lond) 257:398–400
Wieczorek L, Altendorf K (1979) Potassium transport in E. coli: evidence for a K+-transport adenosine-5′-triphosphatase. FEBS Lett 98:233–236
Yap SF, Lim ST (1983) Response of Rhizobium sp. UMKL 20 to NaCl stress. Arch Microbiol 135:224–228
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Lim, S.T. K+-ATPase from Rhizobium sp. UMKL 20. Arch. Microbiol. 142, 393–396 (1985). https://doi.org/10.1007/BF00491910
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DOI: https://doi.org/10.1007/BF00491910