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Regulation of glutamine synthetase ec 6.3.1.2 activity by adenylylation in the gram positive bacterium streptomyces cattleya


, : Regulation of glutamine synthetase ec 6.3.1.2 activity by adenylylation in the gram positive bacterium streptomyces cattleya. Proceedings of the National Academy of Sciences of the United States of America 78(1): 229-233

The enzymatic activity of glutamine synthetase [GS; L-glutamate:ammonia ligase (ADP-forming), EC 6.3.1.2] from the gram-positive bacterium S. cattleya is regulated by covalent modification. In whole cells containing high levels of GS the addition of ammonium chloride leads to a rapid decline in GS activity. Crude extracts prepared from such ammonia-shocked cells had very low levels of GS activity as measured by biosynthetic and .gamma.-glutamyltransferase assays. Incubation of the crude extracts with snake venom phosphodiesterase restored GS activity. In cell extracts, GS was also inactivated by an ATP- and glutamine-dependent reaction. Radioactive labeling studies demonstrated the incorporation of an AMP moiety into GS protein upon modification. The results suggest a covalent modification of GS in a gram-positive bacterium. This modification appears to be adenylylation of the GS subunit similar to that found in the gram-negative bacteria.

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