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Literature summary extracted from

  • Bailly, M.; Blaise, M.; Lorber, B.; Thirup, S.; Kern, D.
    Isolation, crystallization and preliminary X-ray analysis of the transamidosome, a ribonucleoprotein involved in asparagine formation (2009), Acta Crystallogr. Sect. F, 65, 577-581.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.23 for expression in Escherichia coli cells Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.23 a complete dataset of the transamidosome is collected to 3 A resolution Thermus thermophilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.1.1.23 transamidosome the partners involved in tRNA-dependent Asn formation assemble into a ternary complex called the transamidosome, consisting of the ND-AspRS, GatCAD amidotransferase, and tRNAAsn Thermus thermophilus
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Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.1.1.23 300000
-
 ternary complex, transamidosome, ND-AspRS-GatCAB-tRNAAsn, theoretical Thermus thermophilus
6.1.1.23 380000
-
 ternary complex, transamidosome, ND-AspRS-GatCAB-tRNAAsn, determined by gel filtration Thermus thermophilus
6.1.1.23 400000
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 ternary complex, transamidosome, ND-AspRS-GatCAB-tRNAAsn, determined by static light scattering, SLS Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.23 ATP + L-aspartate + tRNAAsn Thermus thermophilus Thermus thermophilus deprived of asparagine synthetase snthesizes Asn on tRNAAsn via a tRNA-dependent pathway involving a nondiscriminating aspartyl-tRNA synthetase that charges Asp onto tRNAAsn prior to conversion of the Asp to Asn by GatCAB AMP + diphosphate + L-aspartyl-tRNAAsn
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 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.23 Thermus thermophilus
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-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.23 the transamidosome complex is isolated by preparative gel filtration on a Superdex G200 column Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.23 ATP + L-aspartate + tRNAAsn Thermus thermophilus deprived of asparagine synthetase snthesizes Asn on tRNAAsn via a tRNA-dependent pathway involving a nondiscriminating aspartyl-tRNA synthetase that charges Asp onto tRNAAsn prior to conversion of the Asp to Asn by GatCAB Thermus thermophilus AMP + diphosphate + L-aspartyl-tRNAAsn
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.23 trimer ternary complex, transamidosome, ND-AspRS-GatCAB-tRNAAsn Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
6.1.1.23 Aspartyl-tRNA synthetase
-
 Thermus thermophilus
6.1.1.23 ND-AspRS
-
 Thermus thermophilus
6.1.1.23 nondiscriminating aspartyl-tRNA synthetase
-
 Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.23 37
-
 activity measurement of the transamidosome Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.23 7.2
-
 activity measurement of the transamidosome Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.23 ATP
-
 Thermus thermophilus