(glutamate—ammonia-ligase) adenylyltransferase
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)] diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]
| [glutamate—ammonia-ligase] adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.42 | ||||||||
| CAS no. | 9077-66-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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
- 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 (3): 535–44. doi:10.1111/j.1432-1033.1970.tb00320.x. 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 (4): 1703–10. doi:10.1073/pnas.58.4.1703. PMC 223983. 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 (3): 452–8. doi:10.1016/0006-291X(66)90182-3. PMID 5338440.
- 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. doi: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 (13): 3769–71. doi:10.1016/S0021-9258(18)97829-4. 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 (2): 239–44. doi:10.1111/j.1432-1033.1972.tb01689.x. PMID 4402680.