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Literature summary extracted from

  • Ibba, M.; Söll, D.
    Aminoacyl-tRNA synthesis (2000), Annu. Rev. Biochem., 69, 617-650.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.5.6 Asp-tRNAAsn + ? Methanothermobacter thermautotrophicus
-
 Asn-tRNAAsn + ?
-
 ?
6.3.5.6 Asp-tRNAAsn + ? Thermus thermophilus AdT is related to the biosynthesis of asparagine rather than to provide charged tRNA for protein biosynthesis Asn-tRNAAsn + ?
-
 ?
6.3.5.6 Asp-tRNAAsn + ? Deinococcus radiodurans AdT is related to the biosynthesis of asparagine rather than to provide charged tRNA for protein biosynthesis Asn-tRNAAsn + ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.6 Aeropyrum pernix
-
-
-
6.3.5.6 Archaeoglobus fulgidus
-
-
-
6.3.5.6 Bacillus subtilis
-
-
-
6.3.5.6 Deinococcus radiodurans
-
-
-
6.3.5.6 Methanocaldococcus jannaschii
-
-
-
6.3.5.6 Methanothermobacter thermautotrophicus
-
 Methanobacterium thermoautotrophicum
-
6.3.5.6 Thermus thermophilus
-
 recombinant enzyme
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.6 Asp-tRNAAsn + ?
-
 Methanothermobacter thermautotrophicus Asn-tRNAAsn + ?
-
 ?
6.3.5.6 Asp-tRNAAsn + ? AdT is related to the biosynthesis of asparagine rather than to provide charged tRNA for protein biosynthesis Thermus thermophilus Asn-tRNAAsn + ?
-
 ?
6.3.5.6 Asp-tRNAAsn + ? AdT is related to the biosynthesis of asparagine rather than to provide charged tRNA for protein biosynthesis Deinococcus radiodurans Asn-tRNAAsn + ?
-
 ?
6.3.5.6 ATP + Asp-tRNAAsn + glutamine
-
 Bacillus subtilis ADP + phosphate + Asn-tRNAAsn + glutamate
-
 ?
6.3.5.6 ATP + Asp-tRNAAsn + glutamine
-
 Methanothermobacter thermautotrophicus ADP + phosphate + Asn-tRNAAsn + glutamate
-
 ?
6.3.5.6 ATP + Asp-tRNAAsn + glutamine
-
 Methanocaldococcus jannaschii ADP + phosphate + Asn-tRNAAsn + glutamate
-
 ?
6.3.5.6 ATP + Asp-tRNAAsn + glutamine
-
 Archaeoglobus fulgidus ADP + phosphate + Asn-tRNAAsn + glutamate
-
 ?
6.3.5.6 ATP + Asp-tRNAAsn + glutamine
-
 Aeropyrum pernix ADP + phosphate + Asn-tRNAAsn + glutamate
-
 ?
6.3.5.6 ATP + Asp-tRNAAsn + glutamine dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT Thermus thermophilus ADP + phosphate + Asn-tRNAAsn + glutamate
-
 ?
6.3.5.6 ATP + Asp-tRNAAsn + glutamine dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT Deinococcus radiodurans ADP + phosphate + Asn-tRNAAsn + glutamate
-
 ?
6.3.5.6 ATP + Glu-tRNAGln + glutamine
-
 Bacillus subtilis ADP + Gln-tRNAGln + glutamate + phosphate
-
 ?
6.3.5.6 ATP + Glu-tRNAGln + glutamine
-
 Methanothermobacter thermautotrophicus ADP + Gln-tRNAGln + glutamate + phosphate
-
 ?
6.3.5.6 ATP + Glu-tRNAGln + glutamine dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT Thermus thermophilus ADP + Gln-tRNAGln + glutamate + phosphate
-
 ?
6.3.5.6 ATP + Glu-tRNAGln + glutamine dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT Deinococcus radiodurans ADP + Gln-tRNAGln + glutamate + phosphate
-
 ?
6.3.5.6 additional information enzyme specificity depends on the biochemical context, i.e. on the availability of the mischarged aminoacyl-tRNA substrate, which is controlled by the presence of a nondiscriminating GluRS or AspRS Thermus thermophilus ?
-
 ?
6.3.5.6 additional information enzyme specificity depends on the biochemical context, i.e. on the availability of the mischarged aminoacyl-tRNA substrate, which is controlled by the presence of a nondiscriminating GluRS or AspRS Deinococcus radiodurans ?
-
 ?
6.3.5.6 additional information archaeal enzyme resembles the bacterial Glu/Asp-AdT, but can only amidate Asp-tRNAAsn and not Glu-tRNAGln Methanothermobacter thermautotrophicus ?
-
 ?
6.3.5.6 additional information archaeal enzyme resembles the bacterial Glu/Asp-AdT, but can only amidate Asp-tRNAAsn and not Glu-tRNAGln Methanocaldococcus jannaschii ?
-
 ?
6.3.5.6 additional information archaeal enzyme resembles the bacterial Glu/Asp-AdT, but can only amidate Asp-tRNAAsn and not Glu-tRNAGln Archaeoglobus fulgidus ?
-
 ?
6.3.5.6 additional information archaeal enzyme resembles the bacterial Glu/Asp-AdT, but can only amidate Asp-tRNAAsn and not Glu-tRNAGln Aeropyrum pernix ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.5.6 heterotrimer
-
 Bacillus subtilis
6.3.5.6 heterotrimer
-
 Thermus thermophilus
6.3.5.6 heterotrimer
-
 Deinococcus radiodurans
6.3.5.6 heterotrimer ORFs corresponding to a heterotrimeric amidotransferase resembling the bacterial Glu/Asp-AdT Methanothermobacter thermautotrophicus
6.3.5.6 heterotrimer ORFs corresponding to a heterotrimeric amidotransferase resembling the bacterial Glu/Asp-AdT Methanocaldococcus jannaschii
6.3.5.6 heterotrimer ORFs corresponding to a heterotrimeric amidotransferase resembling the bacterial Glu/Asp-AdT Archaeoglobus fulgidus
6.3.5.6 heterotrimer ORFs corresponding to a heterotrimeric amidotransferase resembling the bacterial Glu/Asp-AdT Aeropyrum pernix