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Literature summary extracted from

  • Morii, M.; Yamauchi, M.; Ichikawa, T.; Fujii, T.; Takahashi, Y.; Asano, S.; Takeguchi, N.; Sakai, H.
    Involvement of the H3O+-Lys-164-Gln-161-Glu-345 charge transfer pathway in proton transport of gastric H+,K+-ATPase (2008), J. Biol. Chem., 283, 16876-16884.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.2.19 expression of wild-type and mutant enzymes in HEK-293 cells, expression analysis, overview Sus scrofa

Protein Variants

EC Number Protein Variants Comment Organism
7.2.2.19 E345D site-directed mutagenesis, the mutant shows no charge transport pathway, the mutant shows unaltered cell surface expression compared to the wild-type enzyme Sus scrofa
7.2.2.19 E345L site-directed mutagenesis, the mutant shows no charge transport pathway, the mutant shows unaltered cell surface expression compared to the wild-type enzyme Sus scrofa
7.2.2.19 E345Q site-directed mutagenesis, the mutant shows an alternative charge transport pathway H3O+-Arg105-Gln161-Gln345, the mutant shows unaltered cell surface expression compared to the wild-type enzyme Sus scrofa
7.2.2.19 K164L site-directed mutagenesis, the mutant shows an alternative charge transport pathway H3O+-Gln161-Glu345, the mutant shows unaltered cell surface expression compared to the wild-type enzyme Sus scrofa
7.2.2.19 Q161L site-directed mutagenesis, the mutant shows no charge transport pathway, the mutant shows unaltered cell surface expression compared to the wild-type enzyme Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.2.19 SCH 28080
-
 Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.2.19 cell surface
-
 Sus scrofa 9986
-
7.2.2.19 plasma membrane
-
 Sus scrofa 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.2.19 K+ activates Sus scrofa
7.2.2.19 Mg2+ required Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.19 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.2.2.19 stomach gastric membrane Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.19 ATP + H2O + H+/in + K+/out
-
 Sus scrofa ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out protons are charge-transferred from the enzyme's alpha-subunit cytosolic side to H2O in sites 2 and 1, the H2O comes from cytosolic medium, and H3O+ in the sites are transported into lumen during the conformational transition from E1P to E2P, charge transfer pathway charge transfer pathway from hydronium ion in cytosolic medium to Glu345 in cation binding site 2: H3O+-Lys164-Gln161-Glu345 Sus scrofa ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + Rb+/out
-
 Sus scrofa ADP + phosphate + H+/out + Rb+/in
-
 ?

Subunits

EC Number Subunits Comment Organism
7.2.2.19 More homology modeling of wild-type and mutant gastric H+,K+-ATPase beta-subunit and molecular dynamics simulation, simulations of charge transfer in wild-type and mutant enzymes, structure comparisons, overview Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
7.2.2.19 gastric H+,K+-ATPase
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.2.2.19 37
-
 assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2.2.19 6.8
-
 assay at Sus scrofa