(glutamate—ammonia-ligase) adenylyltransferase

Class of enzymes [Glutamate—ammonia-ligase] adenylyltransferase bracket [glutamate—ammonia-ligase] adenylyltransferase 2.7.7.42 9077-66-1 0008882 In enzymology, a [glutamate—ammonia-ligase] adenylyltransferase (2.7.7.42) 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. References 1 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. 14 535–44 4920894 10.1111/j.1432-1033.1970.tb00320.x 3 free 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 1703–10 4867671 10.1073/pnas.58.4.1703 4 223983 free Mecke D, Wulff K, Liess K, Holzer H 1966 Characterization of a glutamine synthetase inactivating enzyme from Escherichia coli Biochem. Biophys. Res. Commun. 24 452–8 5338440 10.1016/0006-291X(66)90182-3 3 1966BBRC...24..452M Mecke D, Wulff K, Holzer H 1966 Metabolit-induzierte Inaktivierung von Glutaminsynthetase aus Escherichia coli im zellfreien System Biochim. Biophys. Acta 128 3 559–567 10.1016/0926-6593(66)90016-6 Shapiro BM, Stadtman ER 1968 5'-adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli J. Biol. Chem. 243 3769–71 4298074 13 10.1016/S0021-9258(18)97829-4 free Wolf D, Ebner E, Hinze H 1972 Inactivation, stabilization and some properties of ATP: glutamine synthetase adenylyltransferase from Escherichia coli B Eur. J. Biochem. 25 239–44 4402680 10.1111/j.1432-1033.1972.tb01689.x 2 free Biology no Glutamate-ammonia-ligase Category:Enzymes of known structure