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Literature summary 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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.12 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

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.1.1.12 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

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

Subunits

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