Erythromycin biosynthesis. The 4-pro-S hydride of NADPH is utilized for ketoreduction by both module 5 and module 6 of the 6-deoxyerythronolide B synthase

Bioorg Med Chem Lett. 2001 Jun 18;11(12):1477-9. doi: 10.1016/s0960-894x(00)00529-1.

Abstract

Incubation of chirally deuterated NADPH with 6-deoxyerythronolide B synthase (DEBS) modules 5 and module 6 and analysis of the derived triketide lactones established that the two ketoreductase domains, KR5 and KR6, are both specific for the 4-pro-S hydride of the nicotinamide cofactor.

Publication types

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

MeSH terms

  • Bacteria / enzymology
  • Bacteria / metabolism
  • Catalytic Domain
  • Deuterium
  • Erythromycin / analogs & derivatives*
  • Erythromycin / biosynthesis*
  • Erythromycin / chemistry
  • Gas Chromatography-Mass Spectrometry
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / metabolism*
  • NADP / metabolism*
  • Oxidation-Reduction
  • Protein Structure, Tertiary
  • Substrate Specificity

Substances

  • Multienzyme Complexes
  • 6-deoxyerythronolide B
  • NADP
  • Erythromycin
  • Deuterium