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Literature summary 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

EC Number Protein Variants Comment Organism
6.1.1.12 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.12 additional information
-
 additional information kinetics, thermodynamics of wild-type enzyme and mutant Q199E Escherichia coli
6.1.1.12 0.32
-
 L-Asp
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.12 Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.12 ATP + L-aspartate + tRNAAsp Escherichia coli
-
 AMP + diphosphate + aspartyl-tRNAAsp
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.12 Escherichia coli P21889
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.12 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.12 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
-
 ?
6.1.1.12 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
-
 ?
6.1.1.12 ATP + L-aspartate + tRNAAsp
-
 Escherichia coli AMP + diphosphate + aspartyl-tRNAAsp
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.12 Aspartyl-tRNA synthetase
-
 Escherichia coli
6.1.1.12 AspRS
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.12 ATP
-
 Escherichia coli