Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773

J Antibiot (Tokyo). 2005 Dec;58(12):766-74. doi: 10.1038/ja.2005.104.


NeoA, B, and C encoded in the neomycin biosynthetic gene cluster have been enzymatically confirmed to be responsible to the formation of 2-deoxystreptamine (DOS) in Streptomyces fradiae. NeoC was functionally characterized as 2-deoxy-scyllo-inosose synthase, which catalyzes the carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose. Further, NeoA appeared to catalyze the oxidation of 2-deoxy-scyllo-inosamine (DOIA) with NAD(P)+ forming 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI). Consequently, NeoA was characterized as 2-deoxy-scyllo-inosamine dehydrogenase. Finally, amino-DOI produced by NeoA from DOIA was transformed into DOS by NeoB. Since NeoB (Neo6) was also reported to be L-glutamine:2-deoxy-scyllo-inosose aminotransferase, all the enzymes in the DOS biosynthesis were characterized for the first time.

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / biosynthesis*
  • Carbohydrate Sequence
  • Chromatography, High Pressure Liquid
  • Chromatography, Liquid
  • Hexosamines / biosynthesis
  • Mass Spectrometry
  • Molecular Sequence Data
  • Multigene Family
  • Streptomyces / enzymology*
  • Streptomyces / genetics


  • Anti-Bacterial Agents
  • Hexosamines
  • 2-deoxystreptamine