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| Content Provider | PubMed Central |
|---|---|
| Author | Cimino, Filiberto Anderson, Wayne B. Stadtman, E. R. |
| Abstract | Treatment of unadenylylated glutamine synthetase from Escherichia coli with tetranitromethane or with N-acetylimidazole produces alterations in catalytic parameters that are similar to alterations caused by the physiologically important process of adenylylation. All three modification reactions lead to a change in divalent ion requirement for biosynthetic activity; the unmodified enzyme requires Mg2+ for activity, whereas the modified enzymes exhibit increased activity with Mn2+. The γ-glutamyl transferase activity of the modified enzyme is more sensitive to feedback inhibition by tryptophan, histidine, CTP, and AMP, and to inhibition by Mg2+ or to inactivation by 5 M urea. Finally, the pH optimum for the unmodified enzyme is 7.9, while the modified enzymes are more active at pH 6.8. |
| Starting Page | 564 |
| File Format | |
| ISSN | 10916490 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 2 |
| Volume Number | 66 |
| Language | English |
| Publisher Date | 1970-06-01 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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