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Literature summary for 7.2.2.13 extracted from

  • Goncalves, R.R.; Masui, D.C.; McNamara, J.C.; Mantelatto, F.L.; Garcon, D.P.; Furriel, R.P.; Leone, F.A.
    A kinetic study of the gill (Na+, K+)-ATPase, and its role in ammonia excretion in the intertidal hermit crab, Clibanarius vittatus (2006), Comp. Biochem. Physiol. A, 145A, 346-356.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
NH4+ stimulation, following a single saturation curve. Synergistic effects of K+ and NH4+. Km value 4.5 mM Clibanarius vittatus

Inhibitors

Inhibitors Comment Organism Structure
orthovanadate up to 67% inhibition in absence of NH4+ Clibanarius vittatus
Ouabain up to 67% inhibition in absence of NH4+ Clibanarius vittatus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5
-
ATP low-affinity ATP hydrolyzing site, 25°C, pH 7.5 Clibanarius vittatus

Metals/Ions

Metals/Ions Comment Organism Structure
K+ stimulation, following a single saturation curve. Synergistic effects of K+ and NH4+. Km value 1.5 mM Clibanarius vittatus
Mg2+ stimulation, following a single saturation curve. K0.5 value 0.36 mM Clibanarius vittatus
Na+ stimulation, following a single saturation curve. Km value 7.4 mM Clibanarius vittatus

Organism

Organism UniProt Comment Textmining
Clibanarius vittatus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
gill
-
Clibanarius vittatus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + Na+/in under saturating Mg2+, Na+, and K+ conditions, enzyme exhibits two well-defined ATP hydrolyzing sites. At the high-affinity sites, K0.5 value is 63.8 nmol per l, at the low-affinity sites, hydrolysis follows Michaelis-Menten kinetics Clibanarius vittatus ADP + phosphate + Na+/out
-
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Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.117
-
Ouabain 25°C, pH 7.5 Clibanarius vittatus