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ATPases are a class of enzymes that catalyze the decomposition of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and a free phosphate ion. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life.
Additional recommended knowledge
Transmembrane ATPases import many of the metabolites necessary for cell metabolism and export toxins, wastes, and solutes that can hinder cellular processes. An important example is the sodium-potassium exchanger (or Na+/K+ATPase), which establishes the ionic concentration balance that maintains the cell potential. Another example is the hydrogen potassium ATPase (H+/K+ATPase or gastric proton pump) that acidifies the contents of the stomach.
Besides exchangers, other categories of transmembrane ATPase include co-transporters and pumps (however, some exchangers are also pumps). Some of these, like the Na+/K+ATPase, cause a net flow of charge, but others do not. These are called "electrogenic" and "nonelectrogenic" transporters, respectively.
The coupling between ATP hydrolysis and transport is more or less a strict chemical reaction, in which a fixed number of solute molecules are transported for each ATP molecule that is hydrolyzed; for example, 3 Na+ ions out of the cell and 2 K+ ions inward per ATP hydrolyzed, for the Na+/K+ exchanger.
Transmembrane ATPases harness the chemical potential energy of ATP, because they perform mechanical work: they transport solutes in a direction opposite to their thermodynamically preferred direction of movement—that is, from the side of the membrane where they are in low concentration to the side where they are in high concentration. This process is considered active transport.
For example, the blocking of the vesicular H+-ATPAses would increase the pH inside vesicles and decrease the pH of the cytoplasm.
Transmembrane ATP synthases
The ATP synthase of mitochondria and chloroplasts is an anabolic enzyme that harnesses the energy of a transmembrane proton gradient as an energy source for adding an inorganic phosphate group to a molecule of adenosine diphosphate (ADP) to form a molecule of adenosine triphosphate (ATP).
This enzyme works when a proton moves down the concentration gradient, giving the enzyme a spinning motion. This unique spinning motion bonds ADP and P together to create ATP.
ATP synthase can also function in reverse, that is, use energy released by ATP hydrolysis to pump protons against their thermodynamic gradient.
There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type of ions they transport.
P-ATPases (sometime known as E1-E2 ATPases) are found in bacteria and in a number of eukaryotic plasma membranes and organelles. P-ATPases function to transport a variety of different compounds, including ions and phospholipids, across a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases, each of which transports a specific type of ion: H+, Na+, K+, Mg2+, Ca2+, Ag+ and Ag2+, Zn2+, Co2+, Pb2+, Ni2+, Cd2+, Cu+ and Cu2+. P-ATPases can be composed of one or two polypeptides, and can usually assume two main conformations called E1 and E2.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "ATPase". A list of authors is available in Wikipedia.|