Analysis of the specificity of the AMP-activated protein kinase by site-directed mutagenesis of bacterially expressed 3-hydroxy 3-methylglutaryl-CoA reductase, using a single primer variant of the unique-site-elimination method.

@article{Ching1996AnalysisOT,
  title={Analysis of the specificity of the AMP-activated protein kinase by site-directed mutagenesis of bacterially expressed 3-hydroxy 3-methylglutaryl-CoA reductase, using a single primer variant of the unique-site-elimination method.},
  author={Y P Ching and S P Davies and David Grahame Hardie},
  journal={European journal of biochemistry},
  year={1996},
  volume={237 3},
  pages={
          800-8
        }
}
The specificity of protein kinases is usually examined using synthetic peptide substrates, either designed variants, or, more recently random peptide libraries. However not all protein kinases utilize synthetic peptides efficiently as substrates. Even among those that do, these approaches neglect effects caused by three-dimensional protein conformation, or the existence of determinants remote from the phosphorylation site. To follow up our previous peptide studies on the specificity of the AMP… CONTINUE READING

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