(glutamate-ammonia-ligase) adenylyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a [glutamate-ammonia-ligase] adenylyltransferase (EC 2.7.7.42) 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 [[[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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 2.7.7.42
BRENDA references for 2.7.7.42 (Recommended.)
PubMed references for 2.7.7.42
PubMed Central references for 2.7.7.42
Google Scholar references for 2.7.7.42
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. 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: 1703–10. 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: 452–8. 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: 559–567.
Shapiro BM, Stadtman ER (1968). "5'-adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli". J. Biol. Chem. 243: 3769–71. 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: 239–44. PMID 4402680.