ArticleBiophysical journal2011
Kinetics of K(+) occlusion by the phosphoenzyme of the Na(+),K(+)-ATPase.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Electrostatic Interaction as a Key Modulator of NaThe Journal of membrane biology · 2026Article
- Cholesterol depletion inhibits NaThe Journal of biological chemistry · 2019Article
- Kinetic contribution to extracellular NaFEBS open bio · 2018Article
- Identification of electric-field-dependent steps in the Na(+),K(+)-pump cycle.Biophysical journal · 2014Article
- Kinetic comparisons of heart and kidney Na+,K(+)-ATPases.Biophysical journal · 2012Article
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Investigations of K(+)-occlusion by the phosphoenzyme of Na(+),K(+)-ATPase from shark rectal gland and pig kidney by stopped-flow fluorimetry reveal major differences in the kinetics of the two enzymes. In the case of the pig enzyme, a single K(+)-occlusion step could be resolved with a rate constant of 342 (± 26) s⁻¹. However, in the case of the shark enzyme, two consecutive K(+)-occlusions were detected with rate constants of 391 (± 19) s⁻¹ and 48 (± 2) s⁻¹ at 24°C and pH 7.4. A conformational change of the phosphoenzyme associated with K(+)-occlusion is, thus, the major rate-determining step of the shark enzyme under saturating concentrations of all substrates, whereas for the pig enzyme the major rate-determining step under the same conditions is the E2 → E1 transition and its associated K(+) deocclusion and release to the cytoplasm. The differences in rate constants of the K(+) occlusion reactions of the two enzymes are paralleled by compensating changes to the rate constant for the E2 → E1 transition, which explains why the differences in the enzymes' kinetic behaviors have not previously been identified.
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