Origin and Evolution of Very Early Sequence Motifs in Enzymes

  • H. Baltscheffsky
  • B. Persson
  • A. Schultz
  • J. R. Pérez-CastiÑeira
  • Margareta Baltscheffsky
Part of the Cellular Origin and Life in Extreme Habitats and Astrobiology book series (COLE, volume 7)

Abstract

Conserved amino acid sequence motifs inenzymes often indicate involvement in the binding of metal ion(s) and/or in the binding and/or reactions of substrate(s). The four very early proteinaceous amino acids are glycine (G), alanine (A), aspartic acid (D) and valine (V) as was demonstrated with the clarification of the stepwise evolution of the genetic code (Eigen and Schuster, 1979), and in agreement with the quantities obtained in the earlier, classical work (Miller, 1953 and on) showing proteinaceous amino acid production under possible prebiotic conditions. Aspartic acid stands out as the unique very early amino acid containing an additional, highly reactive free charge, suitable i.a. for cation binding. Active site motifs with a very high content of any or all of these four amino acids may well be of early evolutionary significance.

Keywords

Genetic Code Lyme Disease Rhodospirillum Rubrum Active Site Motif Putative Active Site 
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 Science+Business Media Dordrecht 2004

Authors and Affiliations

  • H. Baltscheffsky
    • 1
  • B. Persson
    • 2
    • 3
  • A. Schultz
    • 1
  • J. R. Pérez-CastiÑeira
    • 4
  • Margareta Baltscheffsky
    • 1
  1. 1.Department of Biochemistry and Biophysics, Arrhenius LaboratoriesStockholm UniversityStockholmSweden
  2. 2.IFM BioinformaticsLinköping UniversityStockholmSweden
  3. 3.Centre for Genomics and BioinformaticsKarolinska InstitutetStockholmSweden
  4. 4.Instituto de Bioquímica Vegetaly FotosíntesisCSIC-Universidad de SevillaSevillaSpain

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