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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1970 Jun;66(2):564–571. doi: 10.1073/pnas.66.2.564

Ability of Nonenzymic Nitration or Acetylation of E. coli Glutamine Synthetase to Produce Effects Analogous to Enzymic Adenylylation

Filiberto Cimino 1,*, Wayne B Anderson 1,, E R Stadtman 1,
PMCID: PMC283082  PMID: 4317919

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.

Since treatment of the enzyme with N-acetylimidazole results in a decrease in absorbancy at 278 mμ and treatment with tetranitromethane causes an increase in absorbancy at 428 mμ, the effects of these reagents are probably due to modification of certain tyrosyl groups on the enzyme. However, other evidence indicates that the tyrosyl residues which are susceptible to adenylylation in the adenylyltransferase-catalyzed reaction are not involved in the acetylation or nitration reactions.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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