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Conformational and Shape Changes Associated with cAMP- Dependent Protein Kinase

  • Friedrich W. Herberg
  • Susan S. Taylor
Conference paper
  • 79 Downloads
Part of the NATO ASI Series book series (volume 56)

Abstract

Cyclic-AMP dependent protein kinase (cAPK) was one the first discovered protein kinases (Walsh et al., 1968) and is one of the best understood biochemically of the protein kinases (Taylor et al., 1990). cAPK is composed of both regulatory (R) and catalytic (C) subunits. In the absence of cAMP the subunits associate with a high affinity to form an inactive tetrameric (R2C2) holoenzyme. cAMP binds to the R-subunit promoting the dissociation of the complex into a dimeric R-subunit and two monomeric active C-subunits which transfer the γ-phosphate of ATP to a serine or threonine of a peptide or protein substrate (Beebe and Corbin, 1986).

Keywords

Catalytic Subunit Protein Kinase Inhibitor Dependent Protein Kinase Mammalian Enzyme cAMP Binding 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • Friedrich W. Herberg
    • 1
  • Susan S. Taylor
    • 1
  1. 1.Department of ChemistryUniversity of California, San DiegoLa JollaUSA

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