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Literature summary for 6.1.1.12 extracted from

  • Agou, F.; Mirande, M.
    Aspartyl-tRNA synthetase from rat. In vitro functional analysis of its assembly into multisynthetase complex (1997), Eur. J. Biochem., 243, 259-267.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
native recombinant AspRS from rat and the N-terminal truncated derivatives AspRS-DELTA20 and AspRS-DELTA36 expressed in yeast Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
Asp-DELTA20 native recombinant AspRS from rat and the N-terminal truncated derivatives Asp-DELTA20 and AspRS-DELTA36 expressed in yeast. A moderate but significant drop in affinity towards the multisynthetase complex is inferred by the removal of the N-terminal domain. This domain is absolutely required in vivo for association within the multisynthetase structure Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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native recombinant AspRS from rat and the N-terminal truncated derivatives AspRS-DELTA20 and AspRS-DELTA36, expressed in yeast
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + tRNAAsp
-
Rattus norvegicus AMP + diphosphate + L-aspartyl-tRNAAsp
-
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