Significance of the Glutamate-139 Residue of the V-Type Na+-ATPase NtpK Subunit in Catalytic Turnover Linked with Salt Tolerance of Enterococcus hirae
Author:
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference21 articles.
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2. The binding change mechanism for ATP synthase—some probabilities and possibilities;Boyer;Biochim. Biophys. Acta,1993
3. Effects of nigericin and monactin on cation permeability of Streptococcus faecalis and metabolic capacities of potassium-depleted cells;Harold;J. Bacteriol.,1968
4. Extrusion of sodium and hydrogen ions as the primary process in potassium ion accumulation by Streptococcus faecalis;Harold;J. Bacteriol.,1970
5. Deletion analysis of the subunit genes of V-type Na+-ATPase from Enterococcus hirae;Hosaka;J. Biochem.,2006
Cited by 3 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover;Communications Biology;2023-07-28
2. Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover;2022-08-09
3. Mutagenesis of the Residues Forming an Ion Binding Pocket of the NtpK Subunit of Enterococcus hirae V-ATPase;Journal of Bacteriology;2012-06-22
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