Increase in affinity for ATP and change in E1-E2 conformational equilibrium after mutations to the phosphorylation site (Asp369) of the alpha subunit of Na,K-ATPase.
Pedersen
P A
PA
Biomembrane Research Center, August Krogh Institute, University of Copenhagen, Denmark. PAPedersen@aki.ku.dk
Rasmussen
J H
JH
Jørgensen
P L
PL
D000255:Adenosine Triphosphate / Q000378:metabolism*; D001224:Aspartic Acid; D001665:Binding Sites; D007700:Kinetics; D046911:Macromolecular Substances; D016297:Mutagenesis, Site-Directed; D010042:Ouabain / Q000378:metabolism; D010766:Phosphorylation; D017354:Point Mutation; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism*
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D001224:Aspartic Acid; D010042:Ouabain; D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase