(glutamate-ammonia-ligase) adenylyltransferase

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In enzymology, a [glutamate-ammonia-ligase] adenylyltransferase (EC is an enzyme that catalyzes the chemical reaction

ATP + [L-glutamate:ammonia ligase (ADP-forming)] diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]

Thus, the two substrates of this enzyme are ATP and [[[L-glutamate:ammonia ligase (ADP-forming)]]], whereas its two products are diphosphate and [[adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]]].

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase. Other names in common use include glutamine-synthetase adenylyltransferase, ATP:glutamine synthetase adenylyltransferase, and adenosine triphosphate:glutamine synthetase adenylyltransferase.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1V4A.


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  • Ebner E, Wolf D, Gancedo C, Elsasser S, Holzer H (1970). "ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties". Eur. J. Biochem. 14: 535&ndash, 44. PMID 4920894.
  • Kingdon HS, Shapiro BM, Stadtman ER (1967). "Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase". Proc. Natl. Acad. Sci. U. S. A. 58: 1703&ndash, 10. PMID 4867671.
  • Mecke D, Wulff K, Liess K, Holzer H (1966). "Characterization of a glutamine synthetase inactivating enzyme from Escherichia coli". Biochem. Biophys. Res. Commun. 24: 452&ndash, 8. PMID 5338440.
  • Mecke D, Wulff K and Holzer H (1966). "Metabolit-induzierte Inaktivierung von Glutaminsynthetase aus Escherichia coli im zellfreien System". Biochim. Biophys. Acta. 128: 559&ndash, 567.
  • Shapiro BM, Stadtman ER (1968). "5'-adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli". J. Biol. Chem. 243: 3769&ndash, 71. PMID 4298074.
  • Wolf D, Ebner E, Hinze H (1972). "Inactivation, stabilization and some properties of ATP: glutamine synthetase adenylyltransferase from Escherichia coli B". Eur. J. Biochem. 25: 239&ndash, 44. PMID 4402680.

External links

The CAS registry number for this enzyme class is 9077-66-1.

Gene Ontology (GO) codes