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The following other wikis use this file: Usage on ba.wikipedia.org Аденозинтрифосфор кислотаһы — АТФ; Usage on be.wikipedia.org
Most useful ATP analogs cannot be hydrolyzed as ATP would be; instead, they trap the enzyme in a structure closely related to the ATP-bound state. Adenosine 5′-(γ-thiotriphosphate) is an extremely common ATP analog in which one of the gamma-phosphate oxygens is replaced by a sulfur atom; this anion is hydrolyzed at a dramatically slower rate ...
The chemical structure of adenosine triphosphate. Date: 16 August 2007: Source: Self-made in bkchem; edited in perl. Author: Mysid: Other versions: Derivative works of this file: ATP structure revised.png: SVG development
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Molecular structure of adenosine triphosphate (ATP) An ATP-binding motif is a 250-residue sequence within an ATP-binding protein’s primary structure. The binding motif is associated with a protein’s structure and/or function. [1] ATP is a molecule of energy, and can be a coenzyme, involved in a number of biological reactions.
Structure of ATP Structure of ADP Four possible resonance structures for inorganic phosphate. ATP hydrolysis is the catabolic reaction process by which chemical energy that has been stored in the high-energy phosphoanhydride bonds in adenosine triphosphate (ATP) is released after splitting these bonds, for example in muscles, by producing work in the form of mechanical energy.
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Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton 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. [3] [4] The types with this domain include: