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Literature summary for 6.1.1.17 extracted from

  • Hara-Yokoyama, M.; Yokoyama, S.; Miyazawa, T.
    Purification and characterization of glutamyl-tRNA synthetase from an extreme thermophile, Thermus thermophilus HB8 (1984), J. Biochem., 96, 1599-1607.
    View publication on PubMed
Search for more literature for 6.1.1.17

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0006
-
 tRNAGlu substrate from E. coli Thermus thermophilus
0.00065
-
 tRNAGlu substrate from Thermus thermophilus Thermus thermophilus
0.07
-
 L-Glu
-
 Thermus thermophilus
0.23
-
 ATP
-
 Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-
Thermus thermophilus
-
 wild-type and mutant enzymes
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + tRNAGlu
-
 Thermus thermophilus AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
ATP + L-glutamate + tRNAGlu
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
 aminoacylation Thermus thermophilus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 80 about 25% of maximal activity at 50°C and 80°C Thermus thermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 9 h, 30% loss of activity Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9 aminoacylation, in presence of 5 mM Mg2+ Thermus thermophilus