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Literature summary extracted from

  • Nureki, O.; Vassylyev, D.G.; Katayanagi, K.; Shimizu, T.; Sekine, S.i.; Kigawa, T.; Miyazawa, T.; Yokoyama, S.; Morikawa, K.
    Architectures of class-defining and specific domains of glutamyl-tRNA synthetase (1995), Science, 267, 1958-1965.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.17 architectures of class-defining and specific domains Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.17 additional information mutant enzymes with higher Km and lower turnover numbers Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.17 additional information
-
 additional information Km-values of mutant enzymes Thermus thermophilus
6.1.1.17 0.00273
-
 tRNAGlu wild-type enzyme Thermus thermophilus
6.1.1.17 0.023
-
 ATP wild-type enzyme Thermus thermophilus
6.1.1.17 0.12
-
 L-Glu wild-type Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.17 Thermus thermophilus
-
 wild-type and mutant enzymes
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Thermus thermophilus 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 additional information
-
 additional information turnover numbers of wild-type and mutant enzymes Thermus thermophilus