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The sodium–potassium pump (sodium–potassium adenosine triphosphatase, also known as Na + /K +-ATPase, Na + /K + pump, or sodium–potassium ATPase) is an enzyme (an electrogenic transmembrane ATPase) found in the membrane of all animal cells. It performs several functions in cell physiology. The Na + /K +-ATPase enzyme is active (i.e. it ...
The sodium–potassium pump, a critical enzyme for regulating sodium and potassium levels in cells. Sodium ions (Na +) are necessary in small amounts for some types of plants, [1] but sodium as a nutrient is more generally needed in larger amounts [1] by animals, due to their use of it for generation of nerve impulses and for maintenance of electrolyte balance and fluid balance.
The sodium–potassium pump is a critical enzyme for regulating sodium and potassium levels in cells. Potassium is the main intracellular ion for all types of cells, while having a major role in maintenance of fluid and electrolyte balance. [1] [2] Potassium is necessary for the function of all living cells and is thus present in all plant and ...
Knowing the structure of these channels can provide insight into their function and mechanism of gating. They are made up of two different subunits, alpha and beta. The alpha subunit is a tetramer which forms the pore, the voltage sensor, and the calcium sensing region.
The P-type ATPases, also known as E 1-E 2 ATPases, are a large group of evolutionarily related ion and lipid pumps that are found in bacteria, archaea, and eukaryotes. [1] P-type ATPases are α-helical bundle primary transporters named based upon their ability to catalyze auto- (or self-) phosphorylation (hence P) of a key conserved aspartate residue within the pump and their energy source ...
Diffusion vs. Transport. In biology, an ion transporter is a transmembrane protein that moves ions (or other small molecules) across a biological membrane to accomplish many different biological functions, including cellular communication, maintaining homeostasis, energy production, etc. [1] There are different types of transporters including pumps, uniporters, antiporters, and symporters.
Post asked whether the enzyme was inhibited by ouabain. At this stage Skou was unaware that ouabain inhibited the pump, but he immediately telephoned his lab and arranged for the experiment to be done. Ouabain did indeed inhibit the enzyme, thus establishing a link between the enzyme and the sodium-potassium pump. [6]
The crystal structure [17] and function [18] of bacterial members of the IRK-C family have been determined. KirBac1.1, from Burkholderia pseudomallei , is 333 amino acyl residues (aas) long with two N-terminal TMSs flanking a P-loop (residues 1-150), and the C-terminal half of the protein is hydrophilic.