Literature summary for 6.1.1.B3 extracted from

Ray, S.; Blaise, M.; Roy, B.; Ghosh, S.; Kern, D.; Banerjee, R.
Fusion with anticodon binding domain of GluRS is not sufficient to alter the substrate specificity of a chimeric Glu-Q-RS (2014), Protein J., 33, 48-60 .

Search for more literature for 6.1.1.B3

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-glutamate + tRNAAsp	Escherichia coli	the enzyme glutamylates the queuosine Q34 nucleotide of the anticodon of tRNAAsp	AMP + diphosphate + L-glutamyl-tRNAAsp	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-glutamate + tRNAAsp	the enzyme glutamylates the queuosine Q34 nucleotide of the anticodon of tRNAAsp	Escherichia coli	AMP + diphosphate + L-glutamyl-tRNAAsp	-	?
additional information	the enzyme cannot aminoacylate tRNAGlu in vitro	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
Glu-Q-RS	-	Escherichia coli
glutamyl-queuosine-tRNAAsp synthetase	-	Escherichia coli
YadB	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Escherichia coli

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Release 2023.1 (January 2023)