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Literature summary for 6.3.1.2 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

Protein Variants Comment Organism
Y404F mutant lacks adenylylation Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WN39
-
-
Mycobacterium tuberculosis H37Rv P9WN39
-
-
Mycobacterium tuberculosis variant bovis
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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
adenylylation regulation via adenylation, the enzyme is substrate for Escherichia coli adenylyl transferase, but only low adenylylation states are accessible Mycobacterium tuberculosis