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Literature summary for 6.1.1.12 extracted from

  • Cheong, H.K.; Park, J.Y.; Kim, E.H.; Lee, C.; Kim, S.; Kim, Y.; Choi, B.S.; Cheong, C.
    Structure of the N-terminal extension of human aspartyl-tRNA synthetase: implications for its biological function (2003), Int. J. Biochem. Cell Biol., 35, 1548-1557.
    View publication on PubMed
Search for more literature for 6.1.1.12

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate + tRNAAsp Homo sapiens
-
 AMP + diphosphate + L-aspartyl-tRNAAsp
-
 ?
additional information Homo sapiens the N-terminal extension of the enzyme is involved in the transfer of Asp-tRNAAsp to elongation factor alpha1, the structural switch model supports the direct transfer mechanism ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + tRNAAsp
-
 Homo sapiens AMP + diphosphate + L-aspartyl-tRNAAsp
-
 ?
additional information the N-terminal extension of the enzyme is involved in the transfer of Asp-tRNAAsp to elongation factor alpha1, the structural switch model supports the direct transfer mechanism Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
More secondary structure determination, structural switch model, the C-terminus adopts a regular alpha-helix with amphiphilicity, while the N-terminus shows a less-ordered structure with a flexible beta turn Homo sapiens

Synonyms

Synonyms Comment Organism
Aspartic acid translase
-
 Homo sapiens
Aspartyl ribonucleate synthetase
-
 Homo sapiens
aspartyl ribonuleic synthetase
-
 Homo sapiens
Aspartyl-transfer ribonucleic acid synthetase
-
 Homo sapiens
Aspartyl-transfer RNA synthetase
-
 Homo sapiens
Aspartyl-tRNA synthetase
-
 Homo sapiens
DRS
-
 Homo sapiens