(glutamate—ammonia-ligase) adenylyltransferase explained

[glutamate—ammonia-ligase] adenylyltransferase
Ec Number:	2.7.7.42
Cas Number:	9077-66-1
Go Code:	0008882

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

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 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 .

References

• 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 .
• 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 .