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Literature summary for 7.2.2.13 extracted from

  • Crambert, G.; Hasler, U.; Beggah, A.T.; Yu, C.; Modyanov, N.N.; Horisberger, J.D.; Lelievre, L.; Geering, K.
    Transport and pharmacological properties of nine different human Na,K-ATPase isoenzymes (2000), J. Biol. Chem., 275, 1976-1986.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Xenopus oocytes Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
oubain K+ completely abolishes oubain binding to alpha1-beta1 isoenzymes. Residual oubain binding is still observed at high K+ concentrations for alpha2-beta1 and alpha3-beta1 complexes Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
K+ completely abolishes oubain binding to alpha1-beta1 isoenzymes. Residual oubain binding is still observed at high K+ concentrations for alpha2-beta1 and alpha3-beta1 complexes Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + Na+/in + K+/out Homo sapiens enzyme plays a crucial role in cellular ion homeostasis ADP + phosphate + Na+/out + K+/in
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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9 different isoenzymes
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Source Tissue

Source Tissue Comment Organism Textmining
oocyte expression of different isoenzymes in Xenopus oocytes Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Na+/in + K+/out
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Homo sapiens ADP + phosphate + Na+/out + K+/in
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?
ATP + H2O + Na+/in + K+/out enzyme plays a crucial role in cellular ion homeostasis Homo sapiens ADP + phosphate + Na+/out + K+/in
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?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
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additional information
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Homo sapiens