Genes encoding carbocycle-forming enzymes involved in aminoglycoside biosynthesis in deep-sea environmental DNA.
نویسندگان
چکیده
We obtained 19 individual DNA fragments encoding 2-deoxy-scyllo-inosose synthase involved in the biosynthesis of aminoglycoside antibiotics from deep-sea sediments of the Pacific Ocean. Compared with genes from land-based environmental DNA, they showed low diversity. Combined with our previous study concerning the discovery of other aminoglycoside-biosynthetic genes from the same deep-sea samples, we suggest the importance of exploration of multiple biosynthetic genes to determine the diversity of aminoglycoside producers. We found that the deep sea is a useful source for screening of these genes.
منابع مشابه
Exploration of genes that encode a carbocycle-forming enzyme involved in biosynthesis of aminoglycoside antibiotics from the environmental DNA.
2-Deoxy-scyllo-inosose (DOI) synthase is the enzyme participating in biosynthesis of 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics. The gene which encodes the enzyme can be a marker for screening of DOS-containing aminoglycoside-producer and exploration of its biosynthetic gene. Further, this enzyme is expected to be of use in industry, because it converts sugar into 6-membered...
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2-Deoxy-scyllo-inosose (DOI) synthase participates in the biosynthesis of 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics. The enzyme is expected to be of industrial use, because it converts a sustainable resource (glucose 6-phosphate) into carbocycle (DOI), which easily aromatizes to yield catechol. In the present study, we clarified the physiological role of a non-catalytic 20 ...
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Aminoglycoside has been known as a clinically important antibiotic for a long time, but genetic information for the biosynthesis of aminoglycoside is still insufficient. In this study, we tried to clone aminoglycoside-biosynthetic genes from soil DNA for accumulation of genetic information. We chose the genes encoding L-glutamine:(2-deoxy-)scyllo-inosose aminotransferase as the target, because ...
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ورودعنوان ژورنال:
- Bioscience, biotechnology, and biochemistry
دوره 74 5 شماره
صفحات -
تاریخ انتشار 2010