Inactivation of glutamine synthetase by adenylylation in intact cells ofE. coli

✍ Scribed by C. Peter Heinrich; Helmut Holzer

• Publisher: Springer
• Year: 1970
• Tongue: English
• Weight: 385 KB
• Volume: 73
• Category: Article
• ISSN: 0302-8933
• DOI: 10.1007/bf00410312

✦ Synopsis

The glutamine synthetase was inactivated in vivo by incubation of the cell suspension with 2 • 10 -a ~ NH~ + for 2 min. The inactivated glutamine synthetase was extracted from the cells and purified 20-fold.

Incubation of the purified glutamine synthetase with phosphodiesterase regenerated the biosynthetic activity of the enzyme paralleled by the liberation of zaCadenine and 14C-adenosine. laC-adenine and zdC-adenosine were also obtained when inactivated glutamine synthetase, prepared in vitro by use of 14C-ATP and purified adenylylating enzyme, was incubated with phosphodiesterase under the same conditions.

The similar liberation of adenine derivatives by phosphodiesterase from glutamine synthetase inactivated in a cell-free system as well as in intact cells, demonstrates that in both cases the inactivation consists in an adenylylation of the enzyme.