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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Kudo, F; Yamamoto, Y; Yokoyama, K; Eguchi, T; Kakinuma, K

Published Date

  • December 2005

Published In

Volume / Issue

  • 58 / 12

Start / End Page

  • 766 - 774

PubMed ID

  • 16506694

International Standard Serial Number (ISSN)

  • 0021-8820

Digital Object Identifier (DOI)

  • 10.1038/ja.2005.104


  • eng

Conference Location

  • England