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BRENDA support

Literature summary for 7.2.2.19 extracted from

  • Hersey, S.J.; Perez, A.; Matheravidathu, S.; Sachs, G.
    Gastric H+-K+-ATPase in situ: evidence for compartmentalization (1989), Am. J. Physiol., 257, G539-547.
    View publication on PubMed
Search for more literature for 7.2.2.19

Activating Compound

Activating Compound Comment Organism Structure
valinomycin increases ATPase activity Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
Omeprazole acid-activated, irreversible Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information enzyme exists in two distinct compartments. Stimulation of the parietal cells leads to translocation of H+-K+-ATPase from an inactive compartment to a spontaneously active compartment Oryctolagus cuniculus
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Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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Source Tissue

Source Tissue Comment Organism Textmining
gastric gland
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 Oryctolagus cuniculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in + K+/out
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 Oryctolagus cuniculus ADP + phosphate + H+/out + K+/in
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