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

BRENDA support

7.2.2.19: H+/K+-exchanging ATPase

This is an abbreviated version!
For detailed information about H+/K+-exchanging ATPase, go to the full flat file.

Word Map on EC 7.2.2.19

Reaction

ATP
+
H2O
+
H+[side 1]
+
K+[side 2]
=
ADP
+
phosphate
+
H+[side 2]
+
K+[side 1]

Synonyms

(H++K+)-ATPase, Atp12a, ATP1al1, ATP4A, ATP4B, EC 3.6.1.36, EC 3.6.3.10, electroneutral H+/K+-ATPase, gastric (H+, K+)-ATPase, gastric H+,K+-ATPase, gastric H+/K+-ATPase, gastric H+K+-ATPase, gastric H,K-ATPase, gastric H/K-ATPase, gastric HK-ATPase, gastric proton pump, H(+),K(+)-ATPase, H+, K+-ATPase, H+,K+ ATPase, H+,K+-adenosine triphosphatase, H+,K+-ATPase, H+-K+-adenosinetriphosphatase, H+-K+-ATPase, H+-K+-ATPase alpha2, H+/K+ ATPase, H+/K+ pump, H+/K+-ATPase, H+K+-ATPase, H,K-ATPase, H-K-ATPase, HKA, HKalpha1, HKalpha2, HKbeta, More, non-gastric H+/K+ ATPase, non-gastric H+/K+ATPase, non-gastric H,K-ATPase, nongastric H+-K+-ATPase, nongastric H,K-ATPase, nongastric H-K-ATPase, ouabain-sensitive H+/K+-ATPase, Proton pump

ECTree

     7 Translocases
         7.2 Catalysing the translocation of inorganic cations
             7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
                7.2.2.19 H+/K+-exchanging ATPase

Specific Activity

Specific Activity on EC 7.2.2.19 - H+/K+-exchanging ATPase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.07
-
native ouabain-insensitive H+/K+-ATPase from colonic apical plasma membranes, pH not specified in the publication, temperature not specified in the publication
0.186
-
partially purified recombinant enzyme, in presence of 10 mM K+
0.544
-
native ouabain-sensitive H+/K+-ATPase from colonic apical plasma membranes, pH not specified in the publication, temperature not specified in the publication
0.611
-
partially purified recombinant enzyme, in presence of 100 mM Na+
0.626
-
ATP hydrolysis in presence of 10 mM K+ and 0.003 mM valinomycin
0.641
-
ATP hydrolysis in presence of 10 mM K+, 0.1 mM ADP, and 0.003 mM valinomycin
0.685
-
partially purified recombinant enzyme, in presence of 10 mM NH4+
2.045
-
purified native ouabain-sensitive H+/K+-ATPase, pH not specified in the publication, temperature not specified in the publication
2.383
-
in the presence of 2 mM K+, with ATP as substrate, at 37°C
6.3
-
purified enzyme, 40 mM HEPES/Tris, 10 mM KCl, 2 mM MgCl2, 25 mM sucrose, 0.1 mM EGTA/Tris, 2 mM ATP/Tris pH 7.0, at 37°C
7.5
-
purified enzyme, 40 mM HEPES/Tris, 10 mM KCl, 2 mM MgCl2, 25 mM sucrose, 0.1 mM EGTA/Tris, 2 mM ATP/Tris pH 7.0, at 37°C
additional information