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Literature summary for 6.1.1.12 extracted from

  • Mirande, M.; Lazard, M.; Martinez, R.; Latreille, M.T.
    Engineering mammalian aspartyl-tRNA synthetase to probe structural features mediating its association with the multisynthetase complex (1992), Eur. J. Biochem., 203, 459-466.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Chinese hamster ovary cells Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information mutant enzyme with a deletion of 34 amino acids from its N-terminus does not associate within the complex from Chinese hamster ovary cells. A chimeric enzyme made of the amino-terminal moiety of rat liver aspartyl-tRNA synthetase fused to the catalytic domain of yeast lysyl-tRNA synthetase, expressed in Lys-101 cells (a Chinese hamster ovary cell line with a temperature-sensitive lysyl-tRNA synthetase) does not associate within the multisynthetase complex and cannot restore normal growth of mutant cells Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Ovis aries
-
-
-
Rattus norvegicus
-
 wild-type and mutant enzyme with a deletion of 34 amino acids from its N-terminus
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More aspartyl-tRNA synthetase is a component of a multienzyme complex comprising nine aminoacyl-tRNA synthetases Ovis aries