Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.2.2.19 extracted from

  • Witzke, A.; Lindner, K.; Munson, K.; Apell, H.J.
    Inhibition of the gastric H,K-ATPase by clotrimazole (2010), Biochemistry, 49, 4524-4532.
    View publication on PubMed
Search for more literature for 7.2.2.19

Inhibitors

Inhibitors Comment Organism Structure
clotrimazole molecular mechanism of the inhibitory effect is studied by steady-state fluorescence experiments with the electrochromic styryl dye RH421 Sus scrofa
K+ activates, required. But in the presence of 200m M KCl, ion binding sites are more than 99% saturated with K+. The enzyme activity under this condition is near zero Sus scrofa

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
K+ activates, required. But in the presence of 200m M KCl, ion binding sites are more than 99% saturated with K+. The enzyme activity under this condition is near zero Sus scrofa
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
-
 ADP + phosphate + H+/out + K+/in
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native gastric H,K-ATPase from gastric mucosa by a method involving differential and density gradient centrifugation, e.g. sucrose step gradient centrifugation, and plasma vesicle formation oriented as in the parietal cell with the cytoplasmic side outward Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
gastric mucosa
-
 Sus scrofa
-
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 second ion species that can bind to the H,K-ATPase in the E1 conformation is K+ that competes with H+. Experimental activity measurement begins with the ion pump in the E1 state after treatment with nigericin Sus scrofa ADP + phosphate + H+/out + K+/in
-
 ?

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
7.2
-
 assay at Sus scrofa