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 | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.5 | - |
ATP | low-affinity ATP hydrolyzing site, 25°C, pH 7.5 | Clibanarius vittatus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Clibanarius vittatus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
gill | - |
Clibanarius vittatus | - |
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 | - |
? |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.117 | - |
Ouabain | 25°C, pH 7.5 | Clibanarius vittatus |