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Literature summary extracted from

  • Lopes, A.; Schmidt Am Busch, M.; Simonson, T.
    Computational design of protein-ligand binding: modifying the specificity of asparaginyl-tRNA synthetase (2010), J. Comput. Chem., 31, 1273-1286.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.22 AsnRS with bound asparaginyladenylate, AsnAMP, X-ray diffraction structure anaylsis at 2.6 A resolution Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.22 additional information
-
 additional information binding kinetics, affinities, and thermidynamics, molecular dynamics simulations, overview Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.22 Mg2+ a single Mg2+ bound to ATP alpha-phosphate Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.22 Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.22 ATP + L-asparagine + tRNAAsn calculations of substrate binding and reaction mechanism, overview Thermus thermophilus AMP + diphosphate + L-asparaginyl-tRNAAsn
-
 ?
6.1.1.22 additional information analysis of the molecular mechanism by molecular dynamics simulations and computational calculations using wild-type andmutant enzymes, overview Thermus thermophilus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.22 AsnRS
-
 Thermus thermophilus
6.1.1.22 Asparaginyl-tRNA synthetase
-
 Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.22 ATP a single Mg2+ bound to the ligand's alpha-phosphate Thermus thermophilus