EC number:2.7.7.89

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.7 Nucleotidyltransferases
ID:2.7.7.89
Description:[Glutamine synthetase]-adenylyl-L-tyrosine phosphorylase.
Cath: 1.10.4050.10; 1.20.120.1510; 1.20.120.330; 3.30.460.10; 3.30.460.100;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.7.89
BRENDA Enzyme Link: BRENDA 2.7.7.89
KEGG Enzyme Link: KEGG2.7.7.89
BioCyc Enzyme Link: BioCyc 2.7.7.89
ExPASy Enzyme Link: ExPASy2.7.7.89
EC2PDB Enzyme Link: EC2PDB 2.7.7.89
ExplorEnz Enzyme Link: ExplorEnz 2.7.7.89
PRIAM enzyme-specific profiles Link: PRIAM 2.7.7.89
IntEnz Enzyme Link: IntEnz 2.7.7.89
MEDLINE Enzyme Link: MEDLINE 2.7.7.89

EC number:2.7.7.89

MSA:

2.7.7.89;
Phylogenetic Tree:

2.7.7.89;
Uniprot:
M-CSA:
RHEA:43716 [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:7]-[OH;+0:8]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[O;H0;+0:8]-[*:7]
Reaction
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References

TitleAuthorsDatePubMed ID
Reversible adenylylation of glutamine synthetase is dynamically counterbalanced during steady-state growth of Escherichia coli.Okano H, Hwa T, Lenz P, Yan D2010 Dec 320887734
The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction.Jaggi R, van Heeswijk WC, Westerhoff HV, Ollis DL, Vasudevan SG1997 Sep 159312015
Purification and functional roles of the P I and P II components of Escherichia coli glutamine synthetase deadenylylation system.Anderson WB, Stadtman ER1971 Apr4934180
Glutamine synthetase deadenylation: a phosphorolytic reaction yielding ADP as nucleotide product.Anderson WB, Stadtman ER1970 Nov 94920873
The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements.Shapiro BM1969 Feb4893578
Association of ATP: glutamine synthetase adenylyltransferase activity with the P1 component of the glutamine synthetase deadenylylation system.Anderson WB, Hennig SB, Ginsburg A, Stadtman ER1970 Nov4249662
Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase.Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL2004 May15130478
Expression, purification, crystallization, and preliminary X-ray analysis of the N-terminal domain of Escherichia coli adenylyl transferase.Xu Y, Wen D, Clancy P, Carr PD, Ollis DL, Vasudevan SG2004 Mar14766310