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An ATPase is a group on [[Enzyme|enzymes]] in which [[ATP|ATP]] is hydrolyzed to [[ADP|ADP]] + [[Phosphate|Pi]]. ATPase is used in a large veriaty of cellular activities from the binding of DnaA to gene to [[amino acid|amino acid]] degradation&nbsp;<ref>( Biochemistry, 6th Edition, Jeremy M. Berg, John L. Tymoczko, Lubert Stryer, W. H. Freeman and Company, New York, 2008)</ref>. ATPase's are often used to pump [[Ions|ions]] across the cell membrane against their concentration gradient, know ions are that show this are [[Hydrogen|H]]<sup>[[Hydrogen|+]]</sup>, [[Sodium|Na]]<sup>[[Sodium|+]]</sup>, [[Copper|Cu]]<sup>[[Copper|2+]]</sup>, some also transport [[Phospholipids|phospholipids]] with [[amino acid|amino acid]] head groups<ref>( Biochemistry, 6th Edition, Jeremy M. Berg, John L. Tymoczko, Lubert Stryer, W. H. Freeman and Company, New York, 2008)</ref>.  
An ATPase is a group on [[Enzyme|enzymes]] in which [[ATP|ATP]] is hydrolyzed to [[ADP|ADP]] + [[Phosphate|Pi]]. ATPase is used in a large veriaty of cellular activities from the binding of DnaA to gene to [[Amino acid|amino acid]] degradation&nbsp;<ref>( Biochemistry, 6th Edition, Jeremy M. Berg, John L. Tymoczko, Lubert Stryer, W. H. Freeman and Company, New York, 2008)</ref>. ATPase's are often used to pump [[Ions|ions]] across the cell membrane against their concentration gradient, know ions are that show this are [[Hydrogen|H]]<sup>[[Hydrogen|+]]</sup>, [[Sodium|Na]]<sup>[[Sodium|+]]</sup>, [[Copper|Cu]]<sup>[[Copper|2+]]</sup>, some also transport [[Phospholipids|phospholipids]] with [[Amino acid|amino acid]] head groups<ref>( Biochemistry, 6th Edition, Jeremy M. Berg, John L. Tymoczko, Lubert Stryer, W. H. Freeman and Company, New York, 2008)</ref>.  


The most commonly know ATPase is the sodium/potassium pump which actively transports three [[sodium|sodium]] ions out of the cell and two [[potassium|potassium]] ions into the cell for each [[ATP|ATP]] that it hydrolyzes setting up an electrochemical gradient&nbsp;<ref>(http://www.weizmann.ac.il/Biological_Chemistry/scientist/Karlish/steve_karlish.pdf , Professor Steven J D Karlish, Weizman institute of science, 2008)</ref>. Without this particular ATPase as with many others the body simply could not function correctly, thus ATPase's are extremely important enzymes within the cell.  
The most commonly know ATPase is the sodium/potassium pump which actively transports three [[Sodium|sodium]] ions out of the cell and two [[Potassium|potassium]] ions into the cell for each [[ATP|ATP]] that it hydrolyzes setting up an electrochemical gradient&nbsp;<ref>(http://www.weizmann.ac.il/Biological_Chemistry/scientist/Karlish/steve_karlish.pdf , Professor Steven J D Karlish, Weizman institute of science, 2008)</ref>. Without this particular ATPase as with many others the body simply could not function correctly, thus ATPase's are extremely important enzymes within the cell.<br>


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=== References  ===
 
=== <u>'''References'''</u> ===


<references />
<references />

Revision as of 13:47, 10 January 2011

An ATPase is a group on enzymes in which ATP is hydrolyzed to ADP + Pi. ATPase is used in a large veriaty of cellular activities from the binding of DnaA to gene to amino acid degradation [1]. ATPase's are often used to pump ions across the cell membrane against their concentration gradient, know ions are that show this are H+, Na+, Cu2+, some also transport phospholipids with amino acid head groups[2].

The most commonly know ATPase is the sodium/potassium pump which actively transports three sodium ions out of the cell and two potassium ions into the cell for each ATP that it hydrolyzes setting up an electrochemical gradient [3]. Without this particular ATPase as with many others the body simply could not function correctly, thus ATPase's are extremely important enzymes within the cell.

References

  1. ( Biochemistry, 6th Edition, Jeremy M. Berg, John L. Tymoczko, Lubert Stryer, W. H. Freeman and Company, New York, 2008)
  2. ( Biochemistry, 6th Edition, Jeremy M. Berg, John L. Tymoczko, Lubert Stryer, W. H. Freeman and Company, New York, 2008)
  3. (http://www.weizmann.ac.il/Biological_Chemistry/scientist/Karlish/steve_karlish.pdf , Professor Steven J D Karlish, Weizman institute of science, 2008)