Protein kinase A: Difference between revisions
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Protein Kinase A (PKA) is a molecule that is dependent on | 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 <ref>Berg J., Tymoczko J and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman.</ref>. 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. | ||
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Revision as of 13:50, 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.
- ↑ Berg J., Tymoczko J and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman.