The Enzyme Database

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Accepted name: [glutamine synthetase] adenylyltransferase
Reaction: ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O4-(5′-adenylyl)-L-tyrosine
Other name(s): glutamine-synthetase adenylyltransferase; ATP:glutamine synthetase adenylyltransferase; adenosine triphosphate:glutamine synthetase adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase; [glutamate—ammonia-ligase] adenylyltransferase
Systematic name: ATP:[glutamine synthetase]-L-tyrosine adenylyltransferase
Comments: This bacterial enzyme adenylates a tyrosine residue of EC, glutamine synthetase. The enzyme is bifunctional, and also catalyses a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC, [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase) [7,8]. The two activities are present on separate domains.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9077-66-1
1.  Ebner, E., Wolf, D., Gancedo, C., Elsasser, S. and Holzer, H. ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties. Eur. J. Biochem. 14 (1970) 535–544. [DOI] [PMID: 4920894]
2.  Kingdon, H.S., Shapiro, B.M. and Stadtman, E.R. 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. USA 58 (1967) 1703–1710. [DOI] [PMID: 4867671]
3.  Mecke, D., Wulff, K. and Holzer, H. Characterization of a glutamine synthetase inactivating enzyme from Escherichia coli. Biochem. Biophys. Res. Commun. 24 (1966) 452–458. [DOI] [PMID: 5338440]
4.  Mecke, D., Wulff, K. and Holzer, H. Metabolit-induzierte Inaktivierung von Glutaminsynthetase aus Escherichia coli im zellfreien System. Biochim. Biophys. Acta 128 (1966) 559–567.
5.  Shapiro, B.M. and Stadtman, E.R. 5′-Adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli. J. Biol. Chem. 243 (1968) 3769–3771. [PMID: 4298074]
6.  Wolf, D., Ebner, E. and Hinze, H. Inactivation, stabilization and some properties of ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Eur. J. Biochem. 25 (1972) 239–244. [DOI] [PMID: 4402680]
7.  Jaggi, R., van Heeswijk, W.C., Westerhoff, H.V., Ollis, D.L. and Vasudevan, S.G. The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction. EMBO J. 16 (1997) 5562–5571. [DOI] [PMID: 9312015]
8.  Xu, Y., Zhang, R., Joachimiak, A., Carr, P.D., Huber, T., Vasudevan, S.G. and Ollis, D.L. Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase. Structure 12 (2004) 861–869. [DOI] [PMID: 15130478]
[EC created 1972, modified 2016]

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