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Literature summary for 7.2.2.19 extracted from

  • Abe, K.; Tani, K.; Fujiyoshi, Y.
    Systematic comparison of molecular conformations of H+,K+-ATPase reveals an important contribution of the A-M2 linker for the luminal gating (2014), J. Biol. Chem., 289, 30590-30601.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.19

Protein Variants

Protein Variants Comment Organism
additional information the fluorescence probe FITC preferentially forms a covalent bond with the epsilon-amino group of the Lys-518 residue, which is embedded in the conserved Lys-518 in the ATP binding site of the N domain. This chemical modification of the Lys residue impairs H+,K+-ATPase activity (1.7% of activity compared with that of mock-treated enzyme) due to a loss of ATP-binding ability Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
SCH28080
-
 Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Sus scrofa 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in + K+/out Sus scrofa
-
 ADP + phosphate + H+/out + K+/in
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
gastric mucosa
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in + K+/out
-
 Sus scrofa ADP + phosphate + H+/out + K+/in
-
 ?

Synonyms

Synonyms Comment Organism
H+,K+-ATPase
-
 Sus scrofa