Mutagenesis of glutamate 820 of the gastric H+,K+-ATPase alpha-subunit to aspartate decreases the apparent ATP affinity.

doi:10.1016/s0005-2736(98)00227-2

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Article

Mutagenesis of glutamate 820 of the gastric H+,K+-ATPase alpha-subunit to aspartate decreases the apparent ATP affinity.

Biochimica et biophysica acta - 12 Jan 1999

Hermsen H P, Swarts H G, Koenderink J B, De Pont J J

Abstract excerpt

Mutagenesis of Glu820, present in the catalytic subunit of gastric H+,K+-ATPase, into an Asp hardly affects K+-stimulated ATPase and K+-stimulated dephosphorylation of the enzyme. The ATP phosphorylation rate of the E820D mutant, however, is rather low and the apparent affinity for ATP in the pho...

Topics

Adenosine Triphosphate
Aspartic Acid
Glutamic Acid
H(+)-K(+)-Exchanging ATPase
Hydrogen-Ion Concentration
Mutagenesis, Site-Directed
Mutation
Phosphorylation
Temperature

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