Open AccessBlasticidin S‐producing Streptomyces morookaensis possesses an enzyme activity which hydrolyzes puromycin
Author(s) -
Nishimura Motohiro,
Matsuo Hiroaki,
Sugiyama Masanori
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07817.x
Subject(s) - puromycin , streptomyces , hydrolysis , chemistry , enzyme , amide , stereochemistry , biochemistry , tyrosine , bacteria , biology , protein biosynthesis , genetics
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 1 H‐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.