Purification and properties of a prokaryote type glutamine synthetase from the bialaphos producer Streptomyces hygroscopicus SF1293

Yoichi Kumada, Eriko Takano, Kozo Nagaoka

    Research output: Contribution to journalArticlepeer-review

    Abstract

    A prokaryote type glutamine synthetase (GS) was purified from a bialaphos (BA)-producing organism, Streptomyces hygroscopicus SF1293 (SF1293). The GS (GS I) consisted of a 55,000 dalton subunit, and its N-terminal amino acid sequence was similar to that of S. coelicolor GS. GS I was highly sensitive to GS inhibitor phosphinothricin (PPT). An increase of GS activity was observed accompanied by BA accumulation. © 1990.
    Original languageEnglish
    Pages (from-to)61-62
    Number of pages1
    JournalJournal of Fermentation and Bioengineering
    Volume70
    Issue number1
    Publication statusPublished - 1990

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