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- W2046426677 abstract "Addition of NH+4 to Streptomyces griseus 2682 cells grown in NO−3 containing medium resulted in a rapid decline in glutamine synthetase activity due to covalent modification of the enzyme. The NH+4 promoted inactivation of the enzyme was inhibited by the ADP-ribosyltransferase inhibitor 3-methoxybenzamide. In the presence of ADP-ribosyltransferase activity the purified glutamine synthetase was also inhibited by NAD+ in a concentration-dependent manner. ADP-ribosylation of glutamine synthetase was demonstrated in vitro by showing the incorporation of labeled ADP-ribose from [α-32P]NAD+ into glutamine synthetase subunits. Beside ADP-ribosylation, adenylylation of glutamine synthetase was also shown in S. griseus since phosphodiesterase I treatment reactivated the enzyme in crude extracts of NH+4-shocked cells. Glutamine synthetase was also inhibited and modified by ATP in crude cellular extracts. These results suggest that in S. griseus 2682 ADP-ribosylation of glutamine synthetase could be an alternative modification to adenylylation to regulate glutamine synthetase activity." @default.
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- W2046426677 date "1994-10-01" @default.
- W2046426677 modified "2023-09-27" @default.
- W2046426677 title "Modification of Glutamine Synthetase in Streptomyces griseus by ADP-Ribosylation and Adenylylation" @default.
- W2046426677 doi "https://doi.org/10.1006/bbrc.1994.2501" @default.
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