A. D. Argoudelis

PALDIMYCINS A AND B AND ANTIBIOTICS 273a2α AND 273a2β

Paldimycin (antibiotic 273a1) and antibiotic 273a2 as well as their individual components, paldimycins A (273a1 alpha) and B (273a1 beta) and antibiotics 273a2 alpha and 273a2 beta were synthesized from paulomycin, paulomycin A and paulomycin B, respectively, by reacting with N-acetyl-L-cysteine. The semisynthetic antibiotics had chromatographic behavior (TLC, HPLC) and physical and chemical properties identical to the properties of the corresponding antibiotics produced by Streptomyces paulus.

Enzymic nucleotidylylation of lincosaminide antibiotics

SummaryFermentations ofStreptomyces coelicolor are known to convert lincosaminide antibiotics to mixtures of their inactive 3-(5′-ribonucleotides). In the present study, lincomycin, clindamycin and pirlimycin were nucleotidylylated and inactivated using crude enzyme preparations ofS. coelicolor. Optimal conversion is known to occur near pH 6 and to require Mg2+ and nucleoside 5′-triphosphates. In descending order of activity, inosine, adenosine, guanosine, cytidine and uridine 5′-triphosphates functioned as cofactors in these nucleotidylylations. In all instances, 90% of maximal conversion occurred within 24 h. When reaction rates were investigated as functions of enzyme protein addition, pirlimycin appeared to be the superior lincosaminide substrate. Antibiotic activities of these inactivation products could be regenerated through the action of phosphodiesterase, EC 3.1.4.1.