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Literature summary for 7.2.2.19 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
Search for more literature for 7.2.2.19

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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

Inhibitors Comment Organism Structure
SCH 28080
-
 Sus scrofa

Localization

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

Metals/Ions

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

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
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
stomach gastric membrane 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
-
 ?
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
-
 ?
ATP + H2O + H+/in + Rb+/out
-
 Sus scrofa ADP + phosphate + H+/out + Rb+/in
-
 ?

Subunits

Subunits Comment Organism
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

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

Temperature Optimum [°C]

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

pH Optimum

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