Literature summary for 2.7.7.87 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.

Search for more literature for 2.7.7.87

Cloned(Commentary)

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
YrdC	-	Escherichia coli

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)