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Literature summary extracted from

  • Harris, K.A.; Jones, V.; Bilbille, Y.; Swairjo, M.A.; Agris, P.F.
    YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase (2011), RNA, 17, 1678-1687.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.87 His6-tagged YrdC protein overexpressed in Escherichia coli Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.87 L-threonine + ATP + bicarbonate Escherichia coli
-
 L-threonylcarbamoyladenylate + diphosphate + H2O threonylcarbamoyladenosine i.e. t6A ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.87 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.87 by Ni-NTA affinity chromatography to a purity of more than 95% by SDS-PAGE Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.87 L-threonine + ATP + bicarbonate
-
 Escherichia coli L-threonylcarbamoyladenylate + diphosphate + H2O threonylcarbamoyladenosine i.e. t6A ?

Subunits

EC Number Subunits Comment Organism
2.7.7.87 More fluorescence quenching data indicate that YrdC recognizes the RNA substrate in a sequence-dependent manner by directly interacting with certain bases Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.7.87 YrdC
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.7.7.87 physiological function YrdC, with many of the properties of a putative threonylcarbamoyl transferase, most likely functions as a component of a heteromultimeric protein complex for threonylcarbamoyladenosine biosynthesis Escherichia coli