Elevated intrinsic reactivity of seryl hydroxyl groups within the linear peptide triads his-xaa-ser or ser-xaa-his

Brian T. Miller, Alexander Kurosky

Research output: Contribution to journalArticle

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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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