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Literature summary for 2.7.7.42 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

Activating Compound Comment Organism Structure
glutamine adenylyltransferase activity Escherichia coli
PII signal transduction protein adenylyltransferase activity Escherichia coli
PII-UMP adenylyl-removing activity Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
glutamine adenylyl-removing activity Escherichia coli
PII signal transduction protein adenylyl-removing activity Escherichia coli
PII-UMP adenylyltransferase activity Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
glutamine synthetase adenylyltransferase
-
Escherichia coli
GS ATase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli

General Information

General Information Comment Organism
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