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Literature summary for 7.2.2.19 extracted from

  • Abe, K.; Tani, K.; Fujiyoshi, Y.
    Structural and functional characterization of H+, K+-ATPase with bound fluorinated phosphate analogs (2010), J. Struct. Biol., 170, 60-68.
    View publication on PubMed
Search for more literature for 7.2.2.19

Inhibitors

Inhibitors Comment Organism Structure
aluminum fluoride reversible inhibition by the fluorinated phosphate analogue, activity is restored by divalent cations, e.g. Mg2+. Structural comparison of H+,K+-ATPase in the E2BeF and E2AlF states, overview Sus scrofa
beryllium fluoride irreversible inhibition by the fluorinated phosphate analogue, activity is not restored by divalent cations, e.g. Mg2+. Electronmicrospoic structure of BeF-bound H+,K+-ATPase at 8 A resolution, and structural comparison of H+,K+-ATPase in the E2BeF and E2AlF states, overview Sus scrofa
magnesium fluoride reversible inhibition by the fluorinated phosphate analogue, activity is restored by divalent cations, e.g. Mg2+ Sus scrofa
additional information mechanism, by which divalent cations, e.g. Mg2+, reactivate the fluorinated phosphate analogue-inhibited H+,K+-ATPase. Mg2+ interacts with the outside of the vesicles, namely the cytoplasmic side of the enzyme, overview. Prevention of the Mg2+-induced reactivation by K+ binding. The magnitude of the Mg2+-induced reactivation is highly pH dependent, whereas the BeF-inhibited enzyme is not affected Sus scrofa
SCH28080 specific H+,K+-ATPase inhibitor Sus scrofa

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on 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 the electroneutral exchange of two cytoplasmic protons for two luminal potassium ions is achieved by the hydrolysis of one ATP molecule ADP + phosphate + H+/out + K+/in
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa P19156
-
-

Source Tissue

Source Tissue Comment Organism Textmining
stomach
-
 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 the electroneutral exchange of two cytoplasmic protons for two luminal potassium ions is achieved by the hydrolysis of one ATP molecule Sus scrofa ADP + phosphate + H+/out + K+/in
-
 ?

Subunits

Subunits Comment Organism
dimer alpha/beta Sus scrofa

Synonyms

Synonyms Comment Organism
H+, K+-ATPase
-
 Sus scrofa
More the enzyme belongs to the the cation-transporting P-type ATPase family 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
7
-
 assay at Sus scrofa

General Information

General Information Comment Organism
physiological function the gastric proton pump, H+,K+-ATPase is the major membrane protein responsible for the gastric acid H+ secretion Sus scrofa