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Reference on EC 2.7.7.89 - [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heilmeyer, L.; Battig, F.; Holzer, H.
Characterization of a glutamine synthetase b activating (deadenylylating) enzyme system in Escherichia coli
Eur. J. Biochem.
9
259-262
1969
Escherichia coli
Manually annotated by BRENDA team
Shapiro, B.M.
The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements
Biochemistry
8
659-670
1969
Escherichia coli
Manually annotated by BRENDA team
Xu, Y.; Zhang, R.; Joachimiak, A.; Carr, P.D.; Huber, T.; Vasudevan, S.G.; Ollis, D.L.
Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase
Structure
12
861-869
2004
Escherichia coli (P30870)
Manually annotated by BRENDA team
Jiang, P.; Pioszak, A.A.; Ninfa, A.J.
Structure-function analysis of glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49) of Escherichia coli
Biochemistry
46
4117-4132
2007
Escherichia coli
Manually annotated by BRENDA team
Jiang, P.; Mayo, A.E.; Ninfa, A.J.
Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and alpha-ketoglutarate
Biochemistry
46
4133-4146
2007
Escherichia coli
Manually annotated by BRENDA team
Jiang, P.; Ninfa, A.J.
Reconstitution of Escherichia coli glutamine synthetase adenylyltransferase from N-terminal and C-terminal fragments of the enzyme
Biochemistry
48
415-423
2009
Escherichia coli
Manually annotated by BRENDA team
Jiang, P.; Peliska, J.; Ninfa, A.
The regulation of Escherichia coli glutamine synthetase revisited: Role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state
Biochemistry
37
12802-12810
1998
Escherichia coli
Manually annotated by BRENDA team
Rhee, S.; Park, S.; Koo, J.
The role of adenylyltransferase and uridylyltransferase in the regulation of glutamine synthetase in Escherichia coli
Curr. Top. Cell. Regul.
27
221-232
1985
Escherichia coli
Manually annotated by BRENDA team
Jaggi, R.; Van Heeswijk, W.; Westerhoff, H.; Ollis, D.; Vasudevan, S.
The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction
EMBO J.
16
5562-5571
1997
Escherichia coli (P30870)
Manually annotated by BRENDA team
Carroll, P.; Pashley, C.; Parish, T.
Functional analysis of GlnE, an essential adenylyl transferase in Mycobacterium tuberculosis
J. Bacteriol.
190
4894-4902
2008
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Son, H.; Rhee, S.
Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII protein and nucleotide sequence of its structural gene
J. Biol. Chem.
262
8690-8695
1987
Escherichia coli
Manually annotated by BRENDA team
Fink, D.; Falke, D.; Wohlleben, W.; Engels, A.
Nitrogen metabolism in Streptomyces coelicolor A3(2): Modification of glutamine synthetase I by an adenylyltransferase
Microbiology
145
2313-2322
1999
Streptomyces coelicolor (Q8CK02), Streptomyces coelicolor A3(2) (Q8CK02)
Manually annotated by BRENDA team
Van Heeswijk, W.; Hoving, S.; Molenaar, D.; Stegeman, B.; Kahn, D.; Westerhoff, H.
An alternative P(II) protein in the regulation of glutamine synthetase in Escherichia coli
Mol. Microbiol.
21
133-146
1996
Escherichia coli (P30870)
Manually annotated by BRENDA team
Xu, Y.; Wen, D.; Clancy, P.; Carr, P.; Ollis, D.; Vasudevan, S.
Expression, purification, crystallization, and preliminary X-ray analysis of the N-terminal domain of Escherichia coli adenylyl transferase
Protein Expr. Purif.
34
142-146
2004
Escherichia coli (P30870)
Manually annotated by BRENDA team
Johnson, P.J.; Shafer, W.M.
The transcriptional repressor, MtrR, of the mtrCDE efflux pump operon of Neisseria gonorrhoeae can also serve as an activator of "off target" gene (glnE) expression
Antibiotics
4
188-197
2015
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA19
Manually annotated by BRENDA team