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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 <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]], therefore they are involved in the Primary [[Active_transport|Active Transport]] of solutes. ATPase is used in a large veriaty of cellular activities from the binding of DnaA to gene to [[Amino acid|amino acid]] degradation <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 <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> | 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 <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> | ||
Revision as of 22:23, 25 November 2014
An ATPase is a group on enzymes in which ATP is hydrolyzed to ADP + Pi, therefore they are involved in the Primary Active Transport of solutes. 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
- ↑ ( Biochemistry, 6th Edition, Jeremy M. Berg, John L. Tymoczko, Lubert Stryer, W. H. Freeman and Company, New York, 2008)
- ↑ ( Biochemistry, 6th Edition, Jeremy M. Berg, John L. Tymoczko, Lubert Stryer, W. H. Freeman and Company, New York, 2008)
- ↑ (http://www.weizmann.ac.il/Biological_Chemistry/scientist/Karlish/steve_karlish.pdf , Professor Steven J D Karlish, Weizman institute of science, 2008)