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Literature summary extracted from

  • Jiang, P.; Ninfa, A.J.
    Reconstitution of Escherichia coli glutamine synthetase adenylyltransferase from N-terminal and C-terminal fragments of the enzyme (2009), Biochemistry, 48, 415-423.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.42 glutamine adenylyltransferase activity Escherichia coli
2.7.7.42 PII signal transduction protein adenylyltransferase activity Escherichia coli
2.7.7.42 PII-UMP adenylyl-removing activity Escherichia coli
2.7.7.89 signal transduction protein PII the protein activators PII and PII-UMP binding to the enzyme domain with the opposing activity, with intramolecular signal transduction by direct interactions between the N-terminal adenylyl-removing catalytic domain and the C-terminal adenylyltransferase catalytic domain Escherichia coli
2.7.7.89 UMP the protein activators PII and PII-UMP binding to the enzyme domain with the opposing activity, with intramolecular signal transduction by direct interactions between the N-terminal adenylyl-removing catalytic domain and the C-terminal adenylyltransferase catalytic domain Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.42
-
 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.42 glutamine adenylyl-removing activity Escherichia coli
2.7.7.42 PII signal transduction protein adenylyl-removing activity Escherichia coli
2.7.7.42 PII-UMP adenylyltransferase activity Escherichia coli
2.7.7.89 glutamine glutamine inhibition of the adenylyl-removing activity involves intramolecular signaling between the adenylyltransferase and adenylyl-removing domains Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.42 ADP + glutamine synthetase Escherichia coli
-
 adenyl-[glutamine synthetase] + phosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.42 Escherichia coli
-
-
-
2.7.7.89 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.42
-
 Escherichia coli

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.7.7.89 the enzyme can be reconstituted from two purified polypeptides that comprise the N-terminal two-thirds of the protein and the C-terminal one-third of the protein. The reconstituted enzyme exhibits normal activation by signal transduction proteon PII. Properties of the reconstituted enzyme are consistent with the protein activators PII and PII-UMP binding to the enzyme domain with the opposing activity, with intramolecular signal transduction by direct interactions between the N-terminal adenylyl-removing catalytic domain and the C-terminal adenylyltransferase catalytic domain Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.42 ADP + glutamine synthetase
-
 Escherichia coli adenyl-[glutamine synthetase] + phosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.7.7.42 glutamine synthetase adenylyltransferase
-
 Escherichia coli
2.7.7.42 GS ATase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.7.42 ATP
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.7.7.42 physiological function the adenylyltransferase and its substrate glutamine synthetase are part of a signal transduction system that includes two additional proteins, uridylyltransferase/uridylyl-removing enzyme and the PII protein Escherichia coli