Abstract
2-Deoxystreptamine (DOS)-containing aminoglycoside–aminocyclitol (AmAc) antibiotics represent the majority of clinically important AmAcs. Biosynthetic investigations of formation of DOS in actinomycetes are limited to the characterization of 2-deoxy- scyllo-inosose synthase, the first step enzyme of the DOS biosynthetic pathway. A gene encoding l-glutamine:2-deoxy- scyllo-inosose aminotransferase ( tbmB) from the tobramycin producer Streptomyces tenebrarius was expressed heterologously in Escherichia coli. The conversions of 2-deoxy- scyllo-inosose to 2-deoxy- scyllo-inosamine and scyllo-inosose to scyllo-inosamine with the activity of TbmB were determined in vitro. The results indicate that tbmB catalyzes the second step of the DOS biosynthetic pathway during the biosynthesis of 2-deoxystreptamine, a subunit of tobramycin, in S. tenebrarius.
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