Unusually large electrostatic field effect of the buried aspartate in serine proteinases: Source of catalytic power

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Abstract

Calculating the electrostatic potential around the Ser–His–Asp catalytic triad in serine proteinases the very important substituent effect of the buried aspartate is revealed. It is found that the strong Coulomb field of this distant but charged side chain considerably enhances the nucleophilicity of the active serine hydroxyl group. The interpretation of the vital importance of aspartate may replace the “charge–relay” hypothesis which seems to be disproved in the light of recent experiments.

Original languageEnglish
Pages (from-to)723-728
Number of pages6
JournalInternational Journal of Quantum Chemistry
Volume23
Issue number2
DOIs
Publication statusPublished - 1983

ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

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