title: Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773.
abstract: 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.
authors.affiliation: Department of Chemistry, Tokyo Institute of Technology, 2-12-1, O-okayama, Meguro-ku, Tokyo 152-8551, Japan.
authors.forename: Fumitaka
authors.initials: F
authors.lastname: Kudo
authors.forename: Yasuhito
authors.initials: Y
authors.lastname: Yamamoto
authors.forename: Kenichi
authors.initials: K
authors.lastname: Yokoyama
authors.forename: Tadashi
authors.initials: T
authors.lastname: Eguchi
authors.forename: Katsumi
authors.initials: K
authors.lastname: Kakinuma
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000096:biosynthesis*; D002240:Carbohydrate Sequence; D002851:Chromatography, High Pressure Liquid; D002853:Chromatography, Liquid; D006595:Hexosamines / Q000096:biosynthesis; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D005810:Multigene Family; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics
chemical_list: D000900:Anti-Bacterial Agents; D006595:Hexosamines; C007265:2-deoxystreptamine