Blasticidin S-producing Streptomyces morookaensis possesses an enzyme activity which hydrolyzes puromycin |
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Authors: | Motohiro Nishimura Hiroaki Matsuo Masanori Sugiyama |
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Affiliation: | Department of Chemical and Biological Engineering, Ube National College of Technology, Tokiwadai, Ube 755, Japan; Institute of Pharmaceutical Sciences, Hiroshima University School of Medicine, Kasumi 1-2-3, Minami-ku, Hiroshima 734, Japan |
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Abstract: | Abstract Puromycin was inactivated without the presence of acetyl coenzyme A when incubated with extracts of blasticidin S-producing Streptomyces morookaensis . 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 -methyl-l-tyrosine moieties, suggesting that S. morookaensis possesses an enzyme activity which hydrolyzes puromycin. |
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Keywords: | Puromycin Blasticidin S Self-resistance Inactivating enzyme O-Methyl-l-tyrosine Streptomyces morookaensis |
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