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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
2.7.7.42
762231
Differential inhibition of adenylylated and deadenylylated forms of M. tuberculosis glutamine synthetase as a drug discovery platform
PLoS ONE
12
e0185068
2017
Mycobacterium tuberculosis
28972974
2.7.7.42
762231
Differential inhibition of adenylylated and deadenylylated forms of M. tuberculosis glutamine synthetase as a drug discovery platform
PLoS ONE
12
e0185068
2017
Mycobacterium tuberculosis H37Rv
28972974
2.7.7.42
687419
A novel peroxiredoxin activity is located within the C-terminal end of Rhodospirillum rubrum adenylyltransferase
J. Bacteriol.
190
434-437
2008
Rhodospirillum rubrum
17951375
2.7.7.42
662218
Adenylylation and catalytic properties of Mycobacterium tuberculosis glutamine synthetase expressed in Escherichia coli versus Mycobacteria
J. Biol. Chem.
279
22477-22482
2004
Escherichia coli
15037612
2.7.7.42
734704
An alternative P(II) protein in the regulation of glutamine synthetase in Escherichia coli
Mol. Microbiol.
21
133-146
1996
Escherichia coli
8843440
2.7.7.42
643329
ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties
Eur. J. Biochem.
14
535-544
1970
Escherichia coli
4920894
2.7.7.42
643329
ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties
Eur. J. Biochem.
14
535-544
1970
Escherichia coli B / ATCC 11303
4920894
2.7.7.42
672243
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
17355125
2.7.7.42
660632
Expression, purification and crystallization of the C-terminal domain of Escherichia coli adenylyltransferase
Acta Crystallogr. Sect. F
F61
663-665
2005
Escherichia coli
16511122
2.7.7.42
734070
Functional analysis of GlnE, an essential adenylyl transferase in Mycobacterium tuberculosis
J. Bacteriol.
190
4894-4902
2008
Mycobacterium tuberculosis
18469098
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