The tylosin biosynthetic cluster from Streptomyces fradiae: genetic organization of the left region

Article Abstract:

The genetic structure of the left region of the tylosin biosynthetic gene cluster from Streptomyces fradiae has been identified using sequence analysis. Eleven genes, 10 of which belong to the biosynthetic cluster, were found to be present in the 12*9 kb region. The putative functions of the proteins encoded by these genes were also determined. In addition, the functional identification of the genes in the proposed tylosin biosynthetic pathway was deduced by database searches and previous genetic complementation studies performed with tylosin idiotrophic mutants blocked at different phases in tylosin biosynthesis.

Biosynthesis, Transferases, Cytochrome P-450

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The tylosin producer, Streptomyces fradiae, contains a second valine dehydrogenase

Article Abstract:

Streptomyces fradiae has yielded a second valine dehydrogenase that acts in conjunction with the first such enzyme detected in the organism. This enzyme exists in nature as a homodimer with a molecular masses of 80,000 and 41,000 for each if its subunits. It acts upon branched and straight-chain amino acids, particularly L-2-aminobutyrate and L-valine, while it also catalyzes reactions of deamino-NAD and 3-pyridinealdehyde-NAD. Its activity is regulated by L-valine and ammonia.

Dehydrogenases, Oxidoreductases

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Two new tailoring enzymes, a glycosyltransferase and an oxygenase, involved in biosynthesis of the angucycline antibiotic urdamycin A in Streptomyces fradiae Tu2717

Article Abstract:

Results describe the urdamycin biosynthetic gene cluster composition and identify the gene products. The product of urdM exhibits similarities to oxygenase and the amino acid sequence of urdGT2 resembles that of glycosyltransferase. Data further indicate that UrdGT2 catalyzes the earliest glycosyltransfer step in urdamycin biosynthesis.

United States, Statistical Data Included, Antibiotics, Physiological aspects, Oxidases

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