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Literature summary extracted from

  • Hara-Yokoyama, M.; Yokoyama, S.; Miyazawa, T.
    Conformation change of tRNAGlu in the complex with glutamyl-tRNA synthetase is required for specific binding of L-glutamate (1986), Biochemistry, 25, 7031-7036.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.17 additional information
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additional information as the KCl concentration is raised from 0 to 100 mM, the Km value for L-glutamate in the reaction with E. coli tRNAGlu is remarkably increased wheras the Km value for glutamate with Thermus thermophilus tRNAGlu is slightly increased Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.17 Thermus thermophilus
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wild-type and mutant enzymes
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.17 ATP + L-glutamate + tRNAGlu in absence of tRNAGlu, GluRS binds to D-glutamate as well as L-glutamate Thermus thermophilus AMP + diphosphate + L-glutamyl-tRNAGlu
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