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Literature summary for 6.1.1.12 extracted from

  • Frugier, M.; Giege, R.
    Yeast aspartyl-tRNA synthetase binds specifically its own mRNA (2003), J. Mol. Biol., 331, 375-383.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Saccharomyces cerevisiae, and expression as His-tagged protein Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information construction of several N-terminal deletion mutants with altered mRNA binding properties, overview Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate + tRNAAsp Saccharomyces cerevisiae
-
AMP + diphosphate + L-aspartyl-tRNAAsp
-
?
additional information Saccharomyces cerevisiae the enzyme also binds to its mRNA via its N-terminal extension of 70 amino acid residues and the anticodon-binding module, which has a regulatory function on the expression of the enzyme ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
dimeric class II aspartyl-tRNA synthetase
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp RNA-binding motif XSKXXLKKXK Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + tRNAAsp
-
Saccharomyces cerevisiae AMP + diphosphate + L-aspartyl-tRNAAsp
-
?
additional information the enzyme also binds to its mRNA via its N-terminal extension of 70 amino acid residues and the anticodon-binding module, which has a regulatory function on the expression of the enzyme Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
dimer modular structure Saccharomyces cerevisiae
More the N-terminal 70 amino acid residues extension protrudes from the anticodon-binding module, it is not essential for acylation activity but contains the RNA-binding motif that promotes non-specific interactions with the tRNAs, it can also interact with the 5'-end of the enzyme's mRNA Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Aspartic acid translase
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Saccharomyces cerevisiae
Aspartyl ribonucleate synthetase
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Saccharomyces cerevisiae
aspartyl ribonuleic synthetase
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Saccharomyces cerevisiae
Aspartyl-transfer ribonucleic acid synthetase
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Saccharomyces cerevisiae
Aspartyl-transfer RNA synthetase
-
Saccharomyces cerevisiae
Aspartyl-tRNA synthetase
-
Saccharomyces cerevisiae
AspRS
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Saccharomyces cerevisiae