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Literature summary for 6.1.1.18 extracted from

  • Yamasaki, S.; Nakamura, S.; Terada, T.; Shimizu, K.
    Mechanism of the difference in the binding affinity of E. coli tRNAGln to glutaminyl-tRNA synthetase caused by noninterface nucleotides in variable loop (2007), Biophys. J., 92, 192-200.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics, tRNA substrate binding: calculation of the enthalpic and entropic contributions to the binding free energy with the molecular mechanics-Poisson-Boltzmann/surface area method, the entropic difference plays an important role in the difference in binding free energies, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamine + tRNAGln Escherichia coli
-
AMP + diphosphate + L-glutaminyl-tRNAGln
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P00962
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamine + tRNAGln
-
Escherichia coli AMP + diphosphate + L-glutaminyl-tRNAGln
-
?
ATP + L-glutamine + tRNAGln wild-type tRNA, and var-AGGUtRNA, mechanism of the difference in the binding affinity of endogenous tRNAGln to the enzyme caused by noninterface nucleotides in variable loop, overview Escherichia coli AMP + diphosphate + L-glutaminyl-tRNAGln
-
?

Subunits

Subunits Comment Organism
More molecular dynamics simulations on wild-type tRNA, var-AGGUtRNA, and tRNA-GlnRS complexes, overview Escherichia coli

Synonyms

Synonyms Comment Organism
GlnRS
-
Escherichia coli
Glutaminyl-tRNA synthetase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli