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Literature summary extracted from

  • Carroll, P.; Pashley, C.; Parish, T.
    Functional analysis of GlnE, an essential adenylyl transferase in Mycobacterium tuberculosis (2008), J. Bacteriol., 190, 4894-4902.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.42 D438Y/R657S/S684K temperature-sensitive mutant Mycobacterium tuberculosis
2.7.7.42 D720A mutation in the adenylylation domain, compromises activity. Strain shows reduced growth rates in the low-ammonia- and glutamine-containing media Mycobacterium tuberculosis
2.7.7.42 D732A mutation in the adenylylation domain, mutation does not completely abrogate the enzyme activity Mycobacterium tuberculosis
2.7.7.42 V921Q temperature-sensitive mutant Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.42 Mycobacterium tuberculosis
-
-
-
2.7.7.42 Mycobacterium tuberculosis H37Rv
-
-
-
2.7.7.89 Mycobacterium tuberculosis
-
-
-
2.7.7.89 Mycobacterium tuberculosis H37Rv
-
-
-

Synonyms

EC Number Synonyms Comment Organism
2.7.7.42 GlnE
-
Mycobacterium tuberculosis
2.7.7.89 GlnE
-
Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.7.7.42 physiological function in the presence of L-methionine sulfoximine, an inhibitor, and glutamine supplementation, a null mutant is able to grow similarly to the wild type. The GlnE mutant is able to survive and grow for extended periods in liquid medium, but not on solid medium, in the absence of glutamine synthetase inhibition Mycobacterium tuberculosis
2.7.7.89 physiological function deletion of the deadenylylation domain has no apparent effect on growth or glutamine synthetase activity. In the presence of L-methionine sulfoximine, an inhibitor, and glutamine supplementation, a null mutant is able to grow similarly to the wild type. The GlnE mutant is able to survive and grow for extended periods in liquid medium, but not on solid medium, in the absence of glutamine synthetase inhibition Mycobacterium tuberculosis