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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
6.3.1.2 Y404F mutant lacks adenylylation Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.42 0.19
-
 ATP adenylation of Mycobacterium tuberculosis [L-glutamate:ammonia ligase (ADP-forming)] expressed in Escherichia coli Escherichia coli
2.7.7.42 0.352
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 ATP adenylation of Mycobacterium tuberculosis [L-glutamate:ammonia ligase (ADP-forming)] Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.42 Escherichia coli
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-
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6.3.1.2 Mycobacterium tuberculosis P9WN39
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6.3.1.2 Mycobacterium tuberculosis H37Rv P9WN39
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6.3.1.2 Mycobacterium tuberculosis variant bovis
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.3.1.2 adenylylation regulation via adenylation, the enzyme is substrate for Escherichia coli adenylyl transferase, adenylylation state of Mycobacterium bovis enzyme is higher than with the enzyme of pathogenic Mycobacterium tuberculosis Mycobacterium tuberculosis variant bovis
6.3.1.2 adenylylation regulation via adenylation, the enzyme is substrate for Escherichia coli adenylyl transferase, but only low adenylylation states are accessible Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.42 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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