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Literature summary for 6.1.1.12 extracted from

  • Ryckelynck, M.; A Paulus, C.; Frugier, M.
    Post-translational modifications guard yeast from misaspartylation (2008), Biochemistry, 47, 12476-12482.
    View publication on PubMed
Search for more literature for 6.1.1.12

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in yeast YBC-603 cells, functional overexpression of GST- and His6-tagged enzyme in Escherichia coli strain Top10. Expression in yeast cells at low copy number, since overexpression is cytotoxic, while moderate AspRS accumulation in the cell is not deleterious Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information proteomic analysis of mutant cells in comparison to wild-type cells Saccharomyces cerevisiae
R485K site-directed mutagenesis, the substitution in the catalytic site completely inhibits aspartylation by impairing ATP binding, this mutant still retains the capacity to be modified and shows the same pattern as wild-type AspRS on the two-dimensional gel, thus the modifications are not the result of autoaspartylation Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
additional information the yeast AspRS initiates retro-inhibition of its expression, overview Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
 tRNAAsp
-
 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Saccharomyces cerevisiae 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 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 the yeast AspRS not only binds and aminoacylates tRNAAsp but also binds its yeast mRNA and initiates retro-inhibition of its expression, overview AMP + diphosphate + L-aspartyl-tRNAAsp
-
 ?
additional information Saccharomyces cerevisiae misaspartylation of tRNAAsn and tRNAGlu does not exist in vivo ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information the enzyme does not perform autoaspartylation in vivo Saccharomyces cerevisiae
no glycoprotein
-
 Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged enzyme from Escherichia coli strain Top10 by glutathione affinity chromatography, the tag is then cleaved of by thrombin, and the enzyme is further purified by adsorption chromatography yielding an AspRS with a short additional amino acid stretch at its N-terminus Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + tRNAAsp the yeast AspRS not only binds and aminoacylates tRNAAsp but also binds its yeast mRNA and initiates retro-inhibition of its expression, overview Saccharomyces cerevisiae AMP + diphosphate + L-aspartyl-tRNAAsp
-
 ?
ATP + L-aspartate + tRNAAsp the yeast enzyme also binds its own mRNA and autoinhibits itself Saccharomyces cerevisiae AMP + diphosphate + L-aspartyl-tRNAAsp
-
 ?
additional information misaspartylation of tRNAAsn and tRNAGlu does not exist in vivo Saccharomyces cerevisiae ?
-
 ?
additional information increased concentrations of AspRS lead to the accumulation of significant amounts of Asp-tRNAAsn and Asp-tRNAGlu in vitro, but not in vivo. The enzyme does not perform autoaspartylation Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
Aspartyl-tRNA synthetase
-
 Saccharomyces cerevisiae
AspRS
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae