Journal
JOURNAL OF NATURAL PRODUCTS
Volume 70, Issue 4, Pages 618-622Publisher
AMER CHEMICAL SOC
DOI: 10.1021/np060605u
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Funding
- NIGMS NIH HHS [R01 GM069320-04, GM69320, R01 GM069320] Funding Source: Medline
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The nonproteinogenic amino acid capreomycidine is the signature residue found in the tuberactinomycin family of antitubercular peptide antibiotics and an important element of the pharmacophore. Recombinant VioG, a single-module peptide synthetase from the viomycin gene cluster cloned from Streptomyces vinaceus (ATCC11861), specifically activates capreomycidine for incorporation into viomycin (tuberactinomycin B). Insertional disruption of the putative hydroxylase gene vioQ resulted in a mutant that accumulated tuberactinomycin O, suggesting that hydroxylation at C-5 of the capreomycidine residue is a post-assembly event. The inactivated chromosomal copy of vioQ could be complemented with a wild-type copy of the gene to restore viomycin production.
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