Protein kinase A: Difference between revisions

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Protein Kinase A&nbsp;(PKA) is a molecule that is dependent on cyclic AMP (cAMP) and without it is deactivated. PKA is involved in signal-transduction pathways and phosphorylates proteins by adding a phosphate group. The molecule consists of two subunits, a regulatory subunit and a calalytic subunit <ref>Berg J., Tymoczko J and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman.</ref>. These subunits are inactive when cAMP&nbsp;is not bound. When cAMP&nbsp;binds to a regulatory subunit a conformational change occurs. This change means that the catalytic subunit becomes active and is no longer inhibited. This means that the protein can now phosphorylate other proteins by removing a phosphate from ATP and adding it to a serine residue on the target protein which in turn leads to a cellular response.  
Protein Kinase A&nbsp;(PKA) is a molecule that is dependent on&nbsp;[[cyclic AMP]] (cAMP) and without it is deactivated. PKA is involved in signal-transduction pathways and phosphorylates proteins by adding a phosphate group. The molecule consists of two subunits, a regulatory subunit and a calalytic subunit <ref>Berg J., Tymoczko J and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman.</ref>. These subunits are inactive when cAMP&nbsp;is not bound. When cAMP&nbsp;binds to a regulatory subunit a conformational change occurs. This change means that the catalytic subunit becomes active and is no longer inhibited. This means that the protein can now phosphorylate other proteins by removing a phosphate from [[ATP]] and adding it to a serine residue on the target protein which in turn leads to a cellular response.  


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Revision as of 13:45, 21 November 2010

Protein Kinase A (PKA) is a molecule that is dependent on cyclic AMP (cAMP) and without it is deactivated. PKA is involved in signal-transduction pathways and phosphorylates proteins by adding a phosphate group. The molecule consists of two subunits, a regulatory subunit and a calalytic subunit [1]. These subunits are inactive when cAMP is not bound. When cAMP binds to a regulatory subunit a conformational change occurs. This change means that the catalytic subunit becomes active and is no longer inhibited. This means that the protein can now phosphorylate other proteins by removing a phosphate from ATP and adding it to a serine residue on the target protein which in turn leads to a cellular response.

  1. Berg J., Tymoczko J and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman.