ATP hydrolysis: Difference between revisions

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The breaking of the phosphoanhydride [[Bond|bond]] releases [[Energy|energy]], which can be used to drive cellular reactions.  
The breaking of the phosphoanhydride [[Bond|bond]] releases [[Energy|energy]], which can be used to drive cellular reactions.  


This is a reversible reaction. ATP can be both formed and [[Hydrolysed|hydrolysed]] by the cellular enzyme [[ATPase|ATPase]]<ref>Li, C.; Ueno, H.; Wantanabe, R.; Noji, H.; Komatsuzaki, T. 'ATP hydrolysis assists phosphate release and promotes reaction ordering in F1-ATPase' (2015). Nature Communications, 6; 10223.</ref>.  
This is a reversible reaction by the addition of water, the process is called condenstion. ATP can be both formed and [[Hydrolysed|hydrolysed]] by the cellular enzyme [[ATPase|ATPase]]<ref>Li, C.; Ueno, H.; Wantanabe, R.; Noji, H.; Komatsuzaki, T. 'ATP hydrolysis assists phosphate release and promotes reaction ordering in F1-ATPase' (2015). Nature Communications, 6; 10223.</ref>.  


=== References  ===
=== References  ===


<references />
<references />

Revision as of 18:06, 22 October 2018

ATP hydrolysis is the catabolic process of adding water (H20) to split a molecule of ATP (Adenose triphosphate) to form ADP (adenosine diphosphate)[1] and an inorganic phopshate group[2].

The breaking of the phosphoanhydride bond releases energy, which can be used to drive cellular reactions.

This is a reversible reaction by the addition of water, the process is called condenstion. ATP can be both formed and hydrolysed by the cellular enzyme ATPase[3].

References

  1. 'How much energy is released in ATP hydrolysis?' http://book.bionumbers.org/how-much-energy-is-released-in-atp-hydrolysis/ (Accessed 21/10/18)
  2. Crofts, A. 'Factors contributing to the free energy hydrolysis of ATP'. (1996). http://www.life.illinois.edu/crofts/bioph354/atp_hydrolysis.html (accessed 21/10/18)
  3. Li, C.; Ueno, H.; Wantanabe, R.; Noji, H.; Komatsuzaki, T. 'ATP hydrolysis assists phosphate release and promotes reaction ordering in F1-ATPase' (2015). Nature Communications, 6; 10223.