Erythromycin A (compound 1) was inactivated by Streptomyces vendargensis ATCC 25507 in fermentation. The inactivation product was isolated and characterized by nuclear magnetic resonance and mass spectroscopy as 2'-(O-[beta-D-glucopyranosyl])erythromycin A (compound 2). The MICs of compounds 1 and 2 were determined. Compound 2 lacked antibiotic activity when tested against several gram-positive pathogens, as well as S. vendargensis.
An enzyme (lincosaminide O-nucleotidyltransferase) that catalyzes 3-(5 '-ribonucleotidylation) of pirlimycin and several other lincosaminide antibiotics has been purified approximately 35-fold from cell-free extracts of Streptomyces coelicolor Miiller NRRL3532 (UC 5240). The crude enzyme was prepared using lysozyme and was treated with MnCl2 and (NH4)2SO4. Final purification was achieved by anion exchange chromatography. The pirlimycin reaction product was verified as being pirlimycin-3-(5'-adenylate) by NMRspectroscopy and MS. As a result of purification, this lincosaminide nucleotidylating and inactivating enzyme was separated from the macrolide phosphorylating enzymealso present in the cell-free extract.Fermentations and cell-free preparations of Streptomyces coelicolor Miiller were reported to bring about inactivation of pirlimycin, lincomycin, and clindamycin through 3-(5'-ribonucleotidylation) (Fig.
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