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Literature summary extracted from

  • Diller, A.; Vagin, O.; Sachs, G.; Apell, H.J.
    Electrogenic partial reactions of the gastric H,K-ATPase (2005), Biophys. J., 88, 3348-3359.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
7.2.2.19 additional information binding and release steps of K+ and H+ in both principal conformations of the ion pump, E1 and P-E2, are electrogenic, whereas the conformation transitions do not contribute significantly to a charge movement wihtin the membrane dielectric Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.2.19 SCH28080 completely blocks enzyme activity Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.2.19 K+ activates, with 0.11 mM as half saturating K+ concentration for both luminal binding sites, above 10 mM reduction of enzyme activity Sus scrofa
7.2.2.19 Na+
-
 Sus scrofa
7.2.2.19 NH4+
-
 Sus scrofa

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 gastric mucosa
-
 Sus scrofa
-
7.2.2.19 stomach
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.2.2.19 2.383
-
 in the presence of 2 mM K+, with ATP as substrate, at 37°C 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
-
 ?

Synonyms

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

pH Range

EC Number pH Minimum pH Maximum Comment Organism
7.2.2.19 6.5 8.5 at pH 6.5 30% and at pH 8.5 less than 1% of all binding sites are occupied by H+ ions Sus scrofa