Literature summary for 6.1.1.17 extracted from

Blaise, M.; Becker, H.D.; Keith, G.; Cambillau, C.; Lapointe, J.; Giege, R.; Kern, D.
A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon (2004), Nucleic Acids Res., 32, 2768-2775.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	the YadB protein displays 34% identity with the catalytic core of glutamy-tRNA synthetase but lacks the anticodon-binding domain	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + Glu + tRNAAsp	the enzyme glutamylates the queuosine residue, a modified nucleoside at the wooble position of the tRNAASp QUC anticodon. The enzyme is not able to glutamylate tRNAAsp isolated from an Escherichia coli tRNA-guanosine transglycosylase minus strain deprived of the capacity to exchange guanosine 34 with queuosine	Escherichia coli	AMP + diphosphate + L-glutamyl-tRNAAsp	-	?

Synonyms

Synonyms	Comment	Organism
glutamyl-Q tRNAASp synthetase	-	Escherichia coli
tRNA modifying enzyme	-	Escherichia coli
YadB	-	Escherichia coli

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Release 2023.1 (January 2023)