Regulation of an Enzyme by Phosphorylation at the Active Site

DOI Web Site 被引用文献5件
  • James H. Hurley
    Department of Biochemistry and Biophysics and Graduate Group in Biophysics, University of California at San Francisco, San Francisco, CA 94143-0448.
  • Antony M. Dean
    Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720.
  • Julie L. Sohl
    Department of Biochemistry and Biophysics and Graduate Group in Biophysics, University of California at San Francisco, San Francisco, CA 94143-0448.
  • Daniel E Koshland
    Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720.
  • Robert M. Stroud
    Department of Biochemistry and Biophysics and Graduate Group in Biophysics, University of California at San Francisco, San Francisco, CA 94143-0448.

書誌事項

公開日
1990-08-31
DOI
  • 10.1126/science.2204109
公開者
American Association for the Advancement of Science (AAAS)

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説明

<jats:p> The isocitrate dehydrogenase of <jats:italic>Escherichia coli</jats:italic> is an example of a ubiquitous class of enzymes that are regulated by covalent modification. In the three-dimensional structure of the enzyme-substrate complex, isocitrate forms a hydrogen bond with Ser <jats:sup>113</jats:sup> , the site of regulatory phosphorylation. The structures of Asp <jats:sup>113</jats:sup> and Glu <jats:sup>113</jats:sup> mutants, which mimic the inactivation of the enzyme by phosphorylation, show minimal conformational changes from wild type, as in the phosphorylated enzyme. Calculations based on observed structures suggest that the change in electrostatic potential when a negative charge is introduced either by phosphorylation or site-directed mutagenesis is sufficient to inactivate the enzyme. Thus, direct interaction at a ligand binding site is an alternative mechanism to induced conformational changes from an allosteric site in the regulation of protein activity by phosphorylation. </jats:p>

収録刊行物

  • Science

    Science 249 (4972), 1012-1016, 1990-08-31

    American Association for the Advancement of Science (AAAS)

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