(glutamate-ammonia-ligase) adenylyltransferase

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

Thus, the two substrates of this enzyme are ATP and ], whereas its two products are diphosphate and ].

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 .

References

• Ebner E, Wolf D, Gancedo C, Elsasser S, Holzer H "ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties". Eur. J. Biochem. 14 535–44.
• Kingdon HS, Shapiro BM, Stadtman ER "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 1703–10.
• Mecke D, Wulff K, Liess K, Holzer H "Characterization of a glutamine synthetase inactivating enzyme from Escherichia coli". Biochem. Biophys. Res. Commun. 24 452–8.
• Mecke D, Wulff K and Holzer H "Metabolit-induzierte Inaktivierung von Glutaminsynthetase aus Escherichia coli im zellfreien System". Biochim. Biophys. Acta 128 559–567.
• Shapiro BM, Stadtman ER "5'-adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli". J. Biol. Chem. 243 3769–71.
• Wolf D, Ebner E, Hinze H "Inactivation, stabilization and some properties of ATP: glutamine synthetase adenylyltransferase from Escherichia coli B". Eur. J. Biochem. 25 239–44.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes