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Literature summary for 7.2.2.13 extracted from

  • Santos, L.C.; Belli, N.M.; Augusto, A.; Masui, D.C.; Leone, F.A.; McNamara, J.C.; Furriel, R.P.
    Gill (Na+,K+)-ATPase in diadromous, freshwater palaemonid shrimps: Species-specific kinetic characteristics and alpha-subunit expression (2007), Comp. Biochem. Physiol. A, 148A, 178-188.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
NH4+ stimulation, synergistic effect of NH4+ and K+. Enzyme exhibits a single K+ binding site, NH4+ binding to a second, exlcusive site Macrobrachium amazonicum

Metals/Ions

Metals/Ions Comment Organism Structure
K+ stimulation, synergistic effect of NH4+ and K+. Enzyme exhibits a single K+ binding site, NH4+ binding to a second, exlcusive site Macrobrachium amazonicum
Mg2+ stimulation Macrobrachium amazonicum
Na+ stimulation Macrobrachium amazonicum

Organism

Organism UniProt Comment Textmining
Macrobrachium amazonicum
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Source Tissue

Source Tissue Comment Organism Textmining
gill Na+K+-ATPase constitutes 80% of total ATPase activity Macrobrachium amazonicum
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3 Na+/in enzyme has a high- and a low-affinity ATP hydrolizing site Macrobrachium amazonicum ADP + phosphate + 3 Na+/out
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