Erythromycin biosynthesis. Highly efficient incorporation of polyketide chain elongation intermediates into 6-deoxyerythronolide B in an engineered Streptomyces host

J Antibiot (Tokyo). 1995 Jul;48(7):647-51. doi: 10.7164/antibiotics.48.647.

Abstract

Feeding of (2S,3R)-[2,3-13C2]-2-methyl-3-hydroxypentanoyl NAC thioester (1a) to the recombinant organism Streptomyces coelicolor CH999/pCK7 harboring the complete set of eryA genes from Saccharopolyspora erythraea encoding the 6-deoxyerythronolide B synthase (DEBS) resulted in the formation of 6-deoxyerythronolide B (2a) labeled with 13C at C-12 and C-13, as evidenced by the appearance of a pair of enhanced and coupled doublets in the 13C NMR spectrum. The level of 13C enrichment was 15-20 atom% 13C, as much as 100 times higher than the usually observed efficiency of incorporation of NAC thioesters into polyketide metabolites. Similar incorporation of (2S,3R)-[3-2H,3-13C]-2-methyl-3-hydroxypentanoyl NAC thioester (1b) gave 6-deoxyerythronolide B (2b) labeled with both 13C and deuterium at C-13. The intact incorporation of both precursors confirms the normal functioning of the recombinant DEBS proteins in the heterologous host.

Publication types

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

MeSH terms

  • DNA, Recombinant
  • Erythromycin / biosynthesis*
  • Molecular Structure
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / metabolism*
  • Peptide Chain Elongation, Translational*
  • Recombinant Proteins / metabolism
  • Saccharopolyspora / genetics
  • Streptomyces / genetics
  • Streptomyces / metabolism*

Substances

  • DNA, Recombinant
  • Multienzyme Complexes
  • Recombinant Proteins
  • Erythromycin