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Comparisons of creatine kinase primary structures

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Abstract

Comparisons of nine creatine kinase sequences show that 67% of the protein sequence is identical among rabbit, rat, mouse, and chicken muscle, rabbit, rat, and chicken brain, and electric organ sequences from two species of electric ray(Torpedo). The extensive homology precludes a facile prediction of active-site residues based on sequence conservation. The sequences are more similar within isozyme types than are the different isozymes from any one species. There are 35 positions in the muscle and brain sequence pairs for three species which differentiate the two forms. TheTorpedo sequences do not fall completely into either of these patterns. Except for homology with partial sequences of other ATP-guanidino phosphotransferases, no significant homology with other protein or nucleic acid sequences in available databases was found. Preliminary secondary structural predictions suggest that the C-terminal half of the protein is likely an α/β-type protein. Placement in the sequence of two peptides found in previous cross-linking studies reveals two stretches of primary structure that are presumably close in space to the reactive Cys-283 and hence close to the active site.

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Authors and Affiliations

  1. Department of Pharmaceutical Chemistry, University of California, San Francisco, California

    Patricia C. Babbitt, George L. Kenyon, Irwin D. Kuntz & Fred E. Cohen

  2. Metabolic Research Unit and Department of Biochemistry and Biophysics, University of California, San Francisco, California

    John D. Baxter & Brian L. West

  3. Du Pont de Nemours and Co., Wilmington, Delaware

    Pamela A. Benfield & Mark L. Pearson

  4. Department of Biochemistry, University of Washington, Seattle, Washington

    Jean D. Buskin & Steven D. Hauschka

  5. Whitaker College, Massachusetts Institute of Technology, Cambridge, Massachusetts

    William A. Gilbert & Scott D. Putney

  6. Institut für Zellbiologie, Hönggerberg, Zurich, Switzerland

    Johann P. Hossle & Jean-C. Perriard

  7. Department of Anatomy, University of California, San Francisco, Calfornia

    Charles P. Ordahl

  8. T-Cell Sciences, Cambridge, Massachusetts

    Lulu A. Pickering

  9. Merck, Sharp and Dohme Research Labs, West Point, Pennsylvania

    Robert A. Ziven

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  1. Patricia C. Babbitt
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  2. George L. Kenyon
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Babbitt, P.C., Kenyon, G.L., Kuntz, I.D. et al. Comparisons of creatine kinase primary structures. J Protein Chem 5, 1–14 (1986). https://doi.org/10.1007/BF01025580

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  • DOI: https://doi.org/10.1007/BF01025580

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