Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase

D. A. Towler, S. R. Eubanks, D. S. Towery, S. P. Adams, L. Glaser

Research output: Contribution to journalArticle

135 Scopus citations

Abstract

Using synthetic octapeptides, we examined the amino-terminal sequence requirements for substrate recognition by myristoyl-CoA:protein N-myristoyl transferase (NMT). NMT is absolutely specific for peptides with amino-terminal Gly residues. Peptides with Asn, Gln, Ser, Val, or Leu penultimate to the amino-terminal Gly were substrates, whereas peptides with Asp, D-Asn, Phe, or Tyr at this position were not myristoylated. Peptides with aromatic residues at this position competitively inhibited myristoylation of substrates, introducing the possibility of developing specific in vivo inhibitors of NMT. Peptides having sequences which correspond to those of known N-myristoyl proteins, including p60(src), appear to be recognized by a single enzyme, and yeast and murine NMT have identical substrate specificities. The catalytic selectivity of NMT for myristoyl transfer accounts for the remarkable acyl chain specificity of this enzyme.

Original languageEnglish (US)
Pages (from-to)1030-1036
Number of pages7
JournalJournal of Biological Chemistry
Volume262
Issue number3
StatePublished - 1987

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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