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Literature summary for 6.1.1.12 extracted from

  • Thompson, D.; Lazennec, C.; Plateau, P.; Simonson, T.
    Ammonium scanning in an enzyme active site. The chiral specificity of aspartyl-tRNA synthetase (2007), J. Biol. Chem., 282, 30856-30868.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Q199E site-directed mutagenesis and molecular dynamics simulation of the mutation, reduction in binding free energy in the simulation in agreement with experiment, overview Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
succinate 50% inhibition at 210 mM Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics, thermodynamics of wild-type enzyme and mutant Q199E Escherichia coli
0.32
-
L-Asp
-
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-aspartate + tRNAAsp Escherichia coli
-
AMP + diphosphate + aspartyl-tRNAAsp
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P21889
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp active site structure, AspRS substrate recognition and chiral specificity of wild-type enzyme and mutant Q199E, substrate binding in regular versus inverted orientation, overview Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-aspartate + tRNAAsp aspartyl-tRNA synthetase can misacylate tRNAAsp with D-aspartate instead of its usual substrate, L-Asp, substrate specificity and molecular dynamics simulations, overview Escherichia coli AMP + diphosphate + D-aspartyl-tRNAAsp
-
?
ATP + L-aspartate + tRNAAsp aspartyl-tRNA synthetase can misacylate tRNAAsp with D-aspartate instead of its usual substrate, L-Asp, substrate specificity and molecular dynamics simulations, overview Escherichia coli AMP + diphosphate + L-aspartyl-tRNAAsp
-
?
ATP + L-aspartate + tRNAAsp
-
Escherichia coli AMP + diphosphate + aspartyl-tRNAAsp
-
?

Synonyms

Synonyms Comment Organism
Aspartyl-tRNA synthetase
-
Escherichia coli
AspRS
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli