Adenosine triphosphate: Difference between revisions

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==Structure==

ATP (reload <scene name='82/824011/Atp_mg/1'>initial scene</scene>) contains a nitrogenous base (adenine <jmol><jmolLink><script> select ATP and base and not (_P or _O); selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>), a sugar (ribose <jmol><jmolLink><script> select ATP and not base; selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>) and the triphosphate group (<jmol><jmolLink><script> select base and (_P or _O); selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>). Within enzyme active sites, the beta and gamma phosphate groups often bind to a magnesium cation which helps negatively charged nucleophiles to approach the negatively charged triphosphate group. The most common <jmol><jmolLink><script> select ATP; wireframe off; select ADP; wireframe 0.3;delay 0.5; select ADP; wireframe off; select ATP; wireframe 0.3;</script><text>hydrolysis reaction of ATP</text></jmolLink> </jmol> yields ADP, but in some reactions the product is AMP.

ATP (reload <scene name='82/824011/Atp_mg/3'>initial scene</scene>) contains a nitrogenous base (adenine <jmol><jmolLink><script> select ATP and base and not (_P or _O); selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>), a sugar (ribose <jmol><jmolLink><script> select ATP and not base; selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>) and the triphosphate group (<jmol><jmolLink><script> select base and (_P or _O); selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>). Within enzyme active sites, the beta and gamma phosphate groups often bind to a magnesium cation which helps negatively charged nucleophiles to approach the negatively charged triphosphate group. The most common <jmol><jmolLink><script> select ATP; wireframe off; select ADP; wireframe 0.3;delay 0.5; select ADP; wireframe off; select ATP; wireframe 0.3;</script><text>hydrolysis reaction of ATP</text></jmolLink> </jmol> yields ADP, but in some reactions the product is AMP.

</StructureSection>

== References ==

Adenosine triphosphate: Difference between revisions

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 ==Structure==
-<StructureSection load='' size='340' side='right' caption='Caption for this structure' scene='82/824011/Atp_mg/1'>
+<StructureSection load='' size='340' side='right' caption='Caption for this structure' scene='82/824011/Atp_mg/3'>
-ATP (reload <scene name='82/824011/Atp_mg/1'>initial scene</scene>) contains a nitrogenous base (adenine <jmol><jmolLink><script> select ATP and base and not (_P or _O); selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>), a sugar (ribose <jmol><jmolLink><script> select ATP and not base; selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>) and the triphosphate group (<jmol><jmolLink><script> select base and (_P or _O); selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>). Within enzyme active sites, the beta and gamma phosphate groups often bind to a magnesium cation which helps negatively charged nucleophiles to approach the negatively charged triphosphate group. The most common <jmol><jmolLink><script> select ATP; wireframe off; select ADP; wireframe 0.3;delay 0.5; select ADP; wireframe off; select ATP; wireframe 0.3;</script><text>hydrolysis reaction of ATP</text></jmolLink> </jmol> yields ADP, but in some reactions the product is AMP.
+ATP (reload <scene name='82/824011/Atp_mg/3'>initial scene</scene>) contains a nitrogenous base (adenine <jmol><jmolLink><script> select ATP and base and not (_P or _O); selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>), a sugar (ribose <jmol><jmolLink><script> select ATP and not base; selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>) and the triphosphate group (<jmol><jmolLink><script> select base and (_P or _O); selectionHalos ON; delay 0.5;selectionHalos OFF;</script><text>☼</text></jmolLink> </jmol>). Within enzyme active sites, the beta and gamma phosphate groups often bind to a magnesium cation which helps negatively charged nucleophiles to approach the negatively charged triphosphate group. The most common <jmol><jmolLink><script> select ATP; wireframe off; select ADP; wireframe 0.3;delay 0.5; select ADP; wireframe off; select ATP; wireframe 0.3;</script><text>hydrolysis reaction of ATP</text></jmolLink> </jmol> yields ADP, but in some reactions the product is AMP.
 </StructureSection>
 == References ==
 <references/>