Post-translational modification of polyketide and nonribosomal peptide synthases

Curr Opin Chem Biol. 1997 Oct;1(3):309-15. doi: 10.1016/s1367-5931(97)80067-1.

Abstract

The past year has witnessed a major advance in the study of polyketide and nonribosomal peptide biosynthesis with the identification of the phosphopantetheinyl transferase enzyme family, enzymes required to produce active, post-translationally modified polyketide and peptide synthases. Phosphopantetheinyl transferases required for fatty acid, peptide and siderophore biosynthesis have been characterized and a consensus sequence noted in order to facilitate future identification of additional proteins catalyzing phosphopantetheinyl transfer.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Fatty Acids / biosynthesis
  • Multienzyme Complexes / metabolism*
  • Peptides / metabolism
  • Protein Processing, Post-Translational*
  • Transferases (Other Substituted Phosphate Groups) / metabolism*

Substances

  • Fatty Acids
  • Multienzyme Complexes
  • Peptides
  • Transferases (Other Substituted Phosphate Groups)
  • holo-(acyl-carrier-protein) synthase