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

被引:43
作者
Kudo, F [1 ]
Yamamoto, Y [1 ]
Yokoyama, K [1 ]
Eguchi, T [1 ]
Kakinuma, K [1 ]
机构
[1] Tokyo Inst Technol, Dept Chem, Meguro Ku, Tokyo 1528551, Japan
关键词
2-deoxy-scyllo-inosose synthase; L-glutamine : 2-deoxy-scyllo-inosose aminotransferase; 2-deoxyscyllo-inosamine dehydrogenase; 2-deoxystreptamine; neomycin biosynthetic gene cluster;
D O I
10.1038/ja.2005.104
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
NeoA, B, and C encoded in the neomycin biosynthetic gene cluster have been enzymatically confirmed to be responsible to the formation of 2deoxystreptamine (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:2deoxy-scyllo-inosose aminotransferase, all the enzymes in the DOS biosynthesis were characterized for the first time.
引用
收藏
页码:766 / 774
页数:9
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