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Literature summary extracted from

  • Paravisi, S.; Fumagalli, G.; Riva, M.; Morandi, P.; Morosi, R.; Konarev, P.V.; Petoukhov, M.V.; Bernier, S.; Chenevert, R.; Svergun, D.I.; Curti, B.; Vanoni, M.A.
    Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution (2009), FEBS J., 276, 1398-1417.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.17 expression in Escherichia coli Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.17 additional information protein is not toxic when overproduced in Escherichia coli cells indicating that it does not catalyze the mischarging of Escherichia coli tRNAGln with l-Glu and that GluRS /tRNAGln recognition is species specific Mycobacterium tuberculosis

General Stability

EC Number General Stability Organism
6.1.1.17 Mycobacterium tuberculosis GluRS is significantly more sensitive than the Escherichia coli form to tryptic and chymotryptic limited proteolysis. Chymotrypsin-sensitive sites are found in the predicted tRNA stem contact domain next to the ATP binding site. Enzyme is fully protected from proteolysis by ATP and glutamol-AMP Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.17 diphosphate competitive to ATP and L-glutamate, uncompetitive to tRNAGlu Mycobacterium tuberculosis
6.1.1.17 glutamol-AMP noncompetitive to ATP and L-glutamate Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.17 0.08
-
 ATP pH 7.3, 37°C Mycobacterium tuberculosis
6.1.1.17 0.7
-
 tRNAGlu pH 7.3, 37°C Mycobacterium tuberculosis
6.1.1.17 2.7
-
 L-glutamate pH 7.3, 37°C Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.17 Mycobacterium tuberculosis P9WFV9
-
-
6.1.1.17 Mycobacterium tuberculosis H37Rv P9WFV9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.17 recombinant enzyme Mycobacterium tuberculosis

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.17 ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu random binding of ATP and L-glutamate to the enzyme-tRNA complex Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Mycobacterium tuberculosis AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Mycobacterium tuberculosis H37Rv AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.17 0.272
-
 ATP pH 7.3, 37°C Mycobacterium tuberculosis
6.1.1.17 0.408
-
 tRNAGlu pH 7.3, 37°C Mycobacterium tuberculosis
6.1.1.17 2.15
-
 L-glutamate pH 7.3, 37°C Mycobacterium tuberculosis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.1.1.17 0.0015
-
 glutamol-AMP substrate ATP, pH 7.3, 37°C Mycobacterium tuberculosis
6.1.1.17 0.0039
-
 glutamol-AMP substrate L-glutamate, pH 7.3, 37°C Mycobacterium tuberculosis
6.1.1.17 0.0039
-
 glutamol-AMP substrate tRNAGlu, pH 7.3, 37°C Mycobacterium tuberculosis
6.1.1.17 0.027
-
 diphosphate substrate ATP, pH 7.3, 37°C Mycobacterium tuberculosis
6.1.1.17 0.101
-
 diphosphate substrate L-glutamate, pH 7.3, 37°C Mycobacterium tuberculosis