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Literature summary for 6.1.1.12 extracted from

  • Thompson, D.; Simonson, T.
    Molecular dynamics simulations show that bound Mg2+ contributes to amino acid and aminoacyl adenylate binding specificity in aspartyl-tRNA synthetase through long range electrostatic interactions (2006), J. Biol. Chem., 281, 23792-23803.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of the 2.6-A resolution crystal structure of Escherichia coli AspRS with bound aspartyl-adenylate, AspAMP, molecular dynamics simulations Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information ligand binding thermodynamics and kinetics, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the co-substrate ATP binds preferentially with three associated Mg2+ cations in an unusual, bent geometry, the Mg2+ cations play a structural role and also participate catalytically in the enzyme reaction, co-binding of the ATP-Mg3+ complex increases the Asp/Asn binding free energy difference Escherichia coli

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, ligand and substrate binding, and reaction mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the co-substrate ATP binds preferentially with three associated Mg2+ cations in an unusual, bent geometry, the Mg2+ cations play a structural role and also participate catalytically in the enzyme reaction, co-binding of the ATP-Mg3+ complex increases the Asp/Asn binding free energy difference, indicating that amino acid discrimination is substrate-assisted, molecular dynamics simulations, overview Escherichia coli ?
-
 ?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
ATP the co-substrate ATP binds preferentially with three associated Mg2+ cations in an unusual, bent geometry, co-binding of the ATP-Mg3+ complex increases the Asp/Asn binding free energy difference Escherichia coli