Blasticidin S-producing Streptomyces morookaensis possesses an enzyme activity which hydrolyzes puromycin

Puromycin was inactivated without the presence of acetyl coenzyme A when incubated with extracts of blasticidin S-producing Streptomyces morookaensis</it>. The two derivatives from puromycin, contained in the reaction mixture, were detected by thin-layer chromatography, purified by high performance liquid chromatography and analyzed for determination of the chemical structures by 1H-nuclear magnetic resonance and positive-ion fast atom bombardment mass spectrometries. The analytical data revealed that puromycin was inactivated by the hydrolysis of amide linkage between the aminonucleoside and 0</it>-methyl-l-tyrosine moieties, suggesting that S. morookaensis</it> possesses an enzyme activity which hydrolyzes puromycin.