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Literature summary for 2.7.7.89 extracted from

  • Jiang, P.; Pioszak, A.A.; Ninfa, A.J.
    Structure-function analysis of glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49) of Escherichia coli (2007), Biochemistry, 46, 4117-4132.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
D173N/D175N complete loss of adenylyl-removing activity, while adenylyltransferase activity is retained Escherichia coli
D463N/P467A/L469G mutant enzyme has approximately one-half to one-third of the adenylyl-removing activity observed with the wild-type enzyme, and this adenylyl-removing activity is inhibited by PII and by glutamine like the wild-type enzyme. The mutant enzyme also has approximately one-half to one-third of the adenylyltransferase activity when compared to the wild-type enzyme, and this activity is regulated normally by glutamine, PII, and PII-UMP Escherichia coli
D701N/D703N complete loss of adenylyltransferase activity, while adenylyl-removing activity is retained Escherichia coli
additional information truncated versions of ATase missing the C-terminal domain lacked both adenylyltransferase and the adenylyl-removing activity, suggesting a role for the C-terminal nucleotidyltransferase domain in both activities. The purified C-terminal nucleotidyltransferase domain and larger polypeptides containing this domain have significant basal AT activity, which is stimulated by glutamine. A truncated enzyme lacking amino acids 456-577 from the central region shows complete loss of adenylyl-removing activity, while adenylyltransferase activity is retained. Mutation converts signal transduction protein PII from an activator to an inhibitor Escherichia coli
R499A/R501A/D505N/P509A/L511G mutant enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity. Mutant exhibits significant basal adenylyltransferase activity in the absence of any activators Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Subunits

Subunits Comment Organism
More the N-terminal nucleotidyltransferase domain of the bifunctional enzyme contains the adenylyl-removing (AR) active site, and the C-terminal nucleotidyltransferase domain contains the adenylyltransferase (AT) active site. The enzyme contains a glutamine binding site, and glutamine increased the affinity for PII. The enzyme appears to contain multiple sites for the binding of PII and PII-UMP Escherichia coli

General Information

General Information Comment Organism
physiological function glutamine synthetase adenylyltransferase regulates the activity of glutamine synthetase by adenylylation, reaction of EC 2.8.8.42, and deadenylylation in response to signals of nitrogen and carbon status Escherichia coli