Biosynthesis of gramicidin S with the aid of dipeptides by gramicidin S synthetase

Eur J Biochem. 1976 Jul 15;66(3):623-6. doi: 10.1111/j.1432-1033.1976.tb10590.x.


Dipeptides L-phenylalanyl-proline, D-phenylalanyl-proline, prolyl-valine, valyl-lysine, lysyl-leucine and leucyl-phenylalanine, derived from the sequence of gramicidin S, are substrates of the gramicidin S synthetase. When any of these dipeptides are used to replace the two corresponding amino acids in the reaction assay, cyclodecapeptide antibiotic synthesis occurs, and requires the whole multienzyme system. Active esters, like the thiophenyl and p-nitrophenyl esters of D-phenylalanyl-proline are unable to promote gramicidin S biosynthesis with the gramicidin S synthetase system or with the heavy enzyme alone.

MeSH terms

  • Amino Acid Isomerases / metabolism*
  • Amino Acid Sequence
  • Chemical Phenomena
  • Chemistry
  • Dipeptides / metabolism*
  • Gramicidin / biosynthesis*
  • Lysine / metabolism
  • Multienzyme Complexes / metabolism*
  • Peptide Synthases / metabolism*


  • Dipeptides
  • Multienzyme Complexes
  • Gramicidin
  • Amino Acid Isomerases
  • Peptide Synthases
  • Lysine