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Literature summary for 2.7.7.42 extracted from

  • Mehta, R.; Pearson, J.T.; Mahajan, S.; Nath, A.; Hickey, M.J.; Sherman, D.R.; Atkins, W.M.
    Adenylylation and catalytic properties of Mycobacterium tuberculosis glutamine synthetase expressed in Escherichia coli versus Mycobacteria (2004), J. Biol. Chem., 279, 22477-22482.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.19
-
 ATP adenylation of Mycobacterium tuberculosis [L-glutamate:ammonia ligase (ADP-forming)] expressed in Escherichia coli Escherichia coli
0.352
-
 ATP adenylation of Mycobacterium tuberculosis [L-glutamate:ammonia ligase (ADP-forming)] Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [L-glutamate:ammonia ligase (ADP-forming)] the site of adenylylation of the Mycobacterium tuberculosis [L-glutamate:ammonia ligase (ADP-forming)] by the Escherichia coli adenylyltransferase is Tyr406. [L-glutamate:ammonia ligase (ADP-forming)] is not adenylylated when obtained directly from Mycobacterium tuberculosis cultures that are not supplemented with glutamine. Upon the addition of glutamine to the cultures, the Mycobacterium tuberculosis enzyme becomes significantly adenylylated (about 30%) Escherichia coli diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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