Na/K-ATPase as an oligomeric ensemble.
Differences in the kinetic behavior and properties of monomeric and oligomeric forms of membrane-bound Na/K-ATPase are analyzed. It is concluded that enzyme molecules within oligomeric complexes are affected by extrinsic signals that result in change of enzyme activity, whereas the individual (protomeric) state is insensitive to these signals. Some of the major factors of such regulation are microviscosity of the lipid environment, reactive oxygen species, and intracellular protein kinases.
Boldyrev
A A
AA
Center for Molecular Medicine and International Biotechnological Center, Lomonosov Moscow State University, Moscow, 119899 Russia. aa_boldyrev@mail.ru
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D004789:Enzyme Activation; D006801:Humans; D007700:Kinetics; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000378:metabolism*; D018384:Oxidative Stress / Q000502:physiology; D011487:Protein Conformation; D011494:Protein Kinases / Q000378:metabolism; D017382:Reactive Oxygen Species / Q000378:metabolism*; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry / Q000378:metabolism*
D008055:Lipids; D008565:Membrane Proteins; D017382:Reactive Oxygen Species; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D000254:Sodium-Potassium-Exchanging ATPase