The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 2.7.7.89     
Accepted name: [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase
Reaction: [glutamine synthetase]-O4-(5′-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP
Other name(s): adenylyl-[glutamine—synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5′-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate—ammonia ligase]-adenylyl-L-tyrosine phosphorylase
Systematic name: [glutamine synthetase]-O4-(5′-adenylyl)-L-tyrosine:phosphate adenylyltransferase
Comments: This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42, [glutamine synthetase] adenylyltransferase) [3,5]. The two activities are present on separate domains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Anderson, W.B. and Stadtman, E.R. Glutamine synthetase deadenylation: a phosphorolytic reaction yielding ADP as nucleotide product. Biochem. Biophys. Res. Commun. 41 (1970) 704–709. [PMID: 4920873]
2.  Anderson, W.B. and Stadtman, E.R. Purification and functional roles of the P I and P II components of Escherichia coli glutamine synthetase deadenylylation system. Arch. Biochem. Biophys. 143 (1971) 428–443. [PMID: 4934180]
3.  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. [PMID: 9312015]
4.  Xu, Y., Wen, D., Clancy, P., Carr, P.D., Ollis, D.L. and Vasudevan, S.G. Expression, purification, crystallization, and preliminary X-ray analysis of the N-terminal domain of Escherichia coli adenylyl transferase. Protein Expr. Purif. 34 (2004) 142–146. [PMID: 14766310]
5.  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. [PMID: 15130478]
[EC 2.7.7.89 created 1972 as EC 3.1.4.15, transferred 2015 to EC 2.7.7.89, modified 2016]
 
 


Data © 2001–2017 IUBMB
Web site © 2005–2017 Andrew McDonald