Elevated Intrinsic Reactivity of Seryl Hydroxyl Groups within the Linear Peptide Triads His-Xaa-Ser or Ser-Xaa-His

B. T. Miller, A. Kurosky

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    19 Scopus citations

    Abstract

    Chemical modification studies of peptide hormones and random peptides have revealed that seryl hydroxyl groups had enhanced reactivity toward acylating reagents when they occurred in the linear triads His-Xaa-Ser or Ser-Xaa-His (Xaa = any amino acid). O-acylation of serine within these triads was achieved by reaction with N-hydroxysuccinimide esters of biotin (NHS-biotin) and succinic anhydride. Seryl residues not occurring in His-Xaa-Ser/Ser-Xaa-His triads showed no reactivity toward NHS-biotin under reaction conditions described. Results of histidine replacement studies and studies of the pH dependence of O-biotinylation indicated that the increased nucleophilicity of the seryl hydroxyl group was due to intramolecular interaction between the seryl and histidyl residues. Our findings provide strong evidence that such triads represent novel consensus motifs in peptides.

    Original languageEnglish (US)
    Pages (from-to)461-467
    Number of pages7
    JournalBiochemical and Biophysical Research Communications
    Volume196
    Issue number1
    DOIs
    StatePublished - Oct 15 1993

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    ASJC Scopus subject areas

    • Molecular Biology
    • Biophysics
    • Biochemistry

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