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首页> 外文期刊>The Journal of Antibiotics: An International Journal >Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773.
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Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773.

机译：苦链霉菌NBRC 12773中三种关键酶的生物合成2-脱氧链胺。

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摘要

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.
机译：已通过酶法确认新霉素生物合成基因簇中编码的NeoA，B和C负责导致链霉菌中的2-deoxystreptamine（DOS）的形成。 NeoC在功能上被表征为2-脱氧-鞘氨醇合酶，它催化从D-葡萄糖-6-磷酸到2-脱氧-鞘氨醇的碳环形成。此外，NeoA似乎可以催化带有NAD（P）+的2-deoxy-scyllo-inosose（DOIA）氧化，形成3-amino-2,3-dideoxy-scyllo-inosose（amino-DOI）。因此，NeoA被表征为2-脱氧-鞘氨醇脱氢酶。最后，NeoA将NeoA从DOIA生产的氨基DOI转化为DOS。由于还报道了NeoB（Neo6）是L-谷氨酰胺：2-脱氧-鞘氨醇氨基转移酶，因此首次表征了DOS生物合成中的所有酶。

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