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Literature summary for 7.2.2.19 extracted from

  • Law, R.J.; Munson, K.; Sachs, G.; Lightstone, F.C.
    An ion gating mechanism of gastric H,K-ATPase based on molecular dynamics simulations (2008), Biophys. J., 95, 2739-2749.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.19

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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 Oryctolagus cuniculus 5737
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in + K+/out Oryctolagus cuniculus gastric H,K-ATPase is an electroneutral transmembrane pump that moves protons from the cytoplasm of the parietal cell into the gastric lumen in exchange for potassium ions. The mechanism of transport against the established electrochemical gradients includes intermediate conformations in which the transferred ions are trapped within the membrane domain of the pump. The pump cycle involves switching between the E1 and E2P states. Molecular dynamics simulations on homology models of the E2P and E1 states amd K+ transport mechanism, overview. Movement of the M1M2 transmembrane segments, and the displacement of residues Q159, E160, Q110, and T152 during the conformational change, as well as the motions of E343 and L346, acted as the cytoplasmic-side gate ADP + phosphate + H+/out + K+/in
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 ?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
oxyntic cell
-
 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
-
 ?
ATP + H2O + H+/in + K+/out gastric H,K-ATPase is an electroneutral transmembrane pump that moves protons from the cytoplasm of the parietal cell into the gastric lumen in exchange for potassium ions. The mechanism of transport against the established electrochemical gradients includes intermediate conformations in which the transferred ions are trapped within the membrane domain of the pump. The pump cycle involves switching between the E1 and E2P states. Molecular dynamics simulations on homology models of the E2P and E1 states amd K+ transport mechanism, overview. Movement of the M1M2 transmembrane segments, and the displacement of residues Q159, E160, Q110, and T152 during the conformational change, as well as the motions of E343 and L346, acted as the cytoplasmic-side gate Oryctolagus cuniculus ADP + phosphate + H+/out + K+/in
-
 ?

Subunits

Subunits Comment Organism
More structure analysis and H,K-ATPase homology modeling, overview Oryctolagus cuniculus

Synonyms

Synonyms Comment Organism
gastric H,K-ATPase
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 Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ATP
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 Oryctolagus cuniculus