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Literature summary for 6.1.1.22 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
Search for more literature for 6.1.1.22

Crystallization (Commentary)

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
AsnRS
-
 Thermus thermophilus
Asparaginyl-tRNA synthetase
-
 Thermus thermophilus

Cofactor

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