Literature summary for 1.2.1.70 extracted from

Schauer, S.; Chaturvedi, S.; Randau, L.; Moser, J.; Kitabatake, M.; Lorenz, S.; Verkamp, E.; Schubert, W.D.; Nakayashiki, T.; Murai, M.; Wall, K.; Thomann, H.U.; Heinz, D.W.; Inokuchi, H.; Soll, D.; Jahn, D.
Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate (2002), J. Biol. Chem., 277, 48657-48663.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
C170S	mutant enzyme with esterase activity 95% of the wild-type activity and reductase activity with 90% of the wild-type activity	Escherichia coli
C50S	mutant enzyme with no esterase and reductase activity	Escherichia coli
C74S	mutant enzyme with esterase activity 110% of the wild-type activity and reductase activity with 120% of the wild-type activity	Escherichia coli
E114K	mutant enzyme with no esterase and reductase activity	Escherichia coli
G106N	mutant enzyme with no esterase and reductase activity	Escherichia coli
G191D	mutant enzyme reveals esterase, 105% of the wild-type activity, but no reductase activity	Escherichia coli
G44C/S105N/A326T	mutant enzyme with no esterase and reductase activity	Escherichia coli
G7D	mutant enzyme with no esterase and reductase activity	Escherichia coli
R314C	mutant enzyme with no esterase and reductase activity	Escherichia coli
S145F	mutant enzyme with no esterase and reductase activity	Escherichia coli
S22L/S164F	mutant enzyme with no esterase and reductase activity	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
1,10-phenanthroline	5 mM, 25% inhibition	Escherichia coli
2,2'-dipyridyl	5 mM, 20% inhibition	Escherichia coli
5,5'-dithiobis(2-nitrobenzoic acid)	1 mM, 80% inhibition	Escherichia coli
Co2+	-	Escherichia coli
EDTA	10 mM, 55% inhibition	Escherichia coli
EGTA	10 mM, 35% inhibition	Escherichia coli
glutamycin	3 mM, 90% inhibition	Escherichia coli
iodoacetamide	0.1 mM, complete inhibition	Escherichia coli
Ni2+	-	Escherichia coli
PtCl4	1 mM, 90% inhibition	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.024	-	L-glutamyl-tRNAGlu	pH 8.1, 37°C	Escherichia coli
0.039	-	NADPH	pH 8.1, 37°C	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	restores activity after treatment with chelating agents	Escherichia coli
Mg2+	stimulates, restores activity after treatment with chelating agents	Escherichia coli
Mn2+	restores activity after treatment with chelating agents	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
48000	-	2 * 48000, homodimer with an extended structure, SDS-PAGE	Escherichia coli
48448	-	2 * 48448, homodimer with an extended structure, electrospray ionization mass spectrometry	Escherichia coli
180000	-	gel filtration	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamyl-tRNAGlu + NADPH + H+	in presence of NADPH, the end product, glutamate-1-semialdehyde is formed. In the absence of NADPH, Escherichia coli GluTR exhibits substrate esterase activity	Escherichia coli	L-glutamate 1-semialdehyde + NADP+ + tRNAGlu	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 48000, homodimer with an extended structure, SDS-PAGE	Escherichia coli
dimer	2 * 48448, homodimer with an extended structure, electrospray ionization mass spectrometry	Escherichia coli

Synonyms

Synonyms	Comment	Organism
GluTR	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.13	-	L-glutamyl-tRNAGlu	pH 8.1, 37°C	Escherichia coli
0.15	-	NADPH	pH 8.1, 37°C	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Escherichia coli

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Release 2023.1 (January 2023)