Literature summary for 1.2.1.70 extracted from

Lueer, C.; Schauer, S.; Virus, S.; Schubert, W.D.; Heinz, D.W.; Moser, J.; Jahn, D.
Glutamate recognition and hydride transfer by Escherichia coli glutamyl-tRNA reductase (2007), FEBS J., 274, 4609-4614.

Search for more literature for 1.2.1.70

Cloned(Commentary)

Cloned (Comment)	Organism
wild-type GluTR and variants produced as N-terminal His6-fusion proteins	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
C50S	inactive	Escherichia coli
E54K	retains 6% reductase and 2% esterase activity	Escherichia coli
H99N	retains 5% reductase and 4% esterase activity	Escherichia coli
Q116L	lacks reductase activity whereas 30% esterase activity is retained	Escherichia coli
R52K	retains 5% reductase and 4% esterase activity	Escherichia coli
R52Q	inactive	Escherichia coli
S109A	retains 28% reductase and 30% esterase activity	Escherichia coli
T49V	retains 10% reductase and 5% esterase activity	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6X1	-	-

Purification (Commentary)

Purification (Comment)	Organism
wild-type GluTR and variants	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutaminyl-tRNAGlu + NADPH + H+	-	Escherichia coli	? + NADP+ + tRNAGlu	-	?
L-glutamyl-tRNAGlu + NADPH + H+	-	Escherichia coli	L-glutamate 1-semialdehyde + NADP+ + tRNAGlu	-	?

Synonyms

Synonyms	Comment	Organism
GluTR	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Escherichia coli

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Release 2023.1 (January 2023)