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 language | English |
|---|---|
| Pages (from-to) | 61-62 |
| Number of pages | 1 |
| Journal | Journal of Fermentation and Bioengineering |
| Volume | 70 |
| Issue number | 1 |
| Publication status | Published - 1990 |