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EC Tree
IUBMB Comments This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway. The route shown in the
diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the alpha-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37.
The taxonomic range for the selected organisms is: Escherichia coli The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glutamyl-trna reductase, glutr, hema1, hema2, glutr1, athema1,
more
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glutamate tRNA reductase
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glutamate-specific tRNA reductase
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glutamyl transfer RNA reductase
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glutamyl-tRNA reductase
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reductase, glutamyl-transfer ribonucleate
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L-glutamate-semialdehyde:NADP+ oxidoreductase (L-glutamyl-tRNAGlu-forming)
This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway. The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the alpha-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37.
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L-glutaminyl-tRNAGlu + NADPH + H+
? + NADP+ + tRNAGlu
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?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
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-
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?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
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?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
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?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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in presence of NADPH, the end product, glutamate-1-semialdehyde is formed. In the absence of NADPH, Escherichia coli GluTR exhibits substrate esterase activity
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?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme interacts directly with the amino-acylated acceptor stem and the D-stem, whereas the anticodon domain serves as a major recognition element of aminoacyl tRNA synthetases
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?
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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
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?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
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?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
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?
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Ca2+
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restores activity after treatment with chelating agents
Mg2+
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stimulates, restores activity after treatment with chelating agents
Mn2+
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restores activity after treatment with chelating agents
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1,10-phenanthroline
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5 mM, 25% inhibition
2,2'-dipyridyl
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5 mM, 20% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
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1 mM, 80% inhibition
EDTA
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10 mM, 55% inhibition
EGTA
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10 mM, 35% inhibition
glutamycin
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3 mM, 90% inhibition
heme
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feedback inhibition
iodoacetamide
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0.1 mM, complete inhibition
PtCl4
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1 mM, 90% inhibition
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0.024
L-glutamyl-tRNAGlu
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pH 8.1, 37°C
0.039
NADPH
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pH 8.1, 37°C
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0.13
L-glutamyl-tRNAGlu
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pH 8.1, 37°C
0.15
NADPH
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pH 8.1, 37°C
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UniProt
brenda
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brenda
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physiological function
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glutamyl-tRNA reductase (GluTR) is the first key enzyme of C5 pathway, it is feedback regulated by heme, and its N-terminus plays a critical role on its stability control
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48000
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2 * 48000, homodimer with an extended structure, SDS-PAGE
48448
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2 * 48448, homodimer with an extended structure, electrospray ionization mass spectrometry
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dimer
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2 * 48000, homodimer with an extended structure, SDS-PAGE
dimer
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2 * 48448, homodimer with an extended structure, electrospray ionization mass spectrometry
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E54K
retains 6% reductase and 2% esterase activity
H99N
retains 5% reductase and 4% esterase activity
Q116L
lacks reductase activity whereas 30% esterase activity is retained
R52K
retains 5% reductase and 4% esterase activity
S109A
retains 28% reductase and 30% esterase activity
T49V
retains 10% reductase and 5% esterase activity
C170S
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mutant enzyme with esterase activity 95% of the wild-type activity and reductase activity with 90% of the wild-type activity
C50S
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mutant enzyme with no esterase and reductase activity
C74S
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mutant enzyme with esterase activity 110% of the wild-type activity and reductase activity with 120% of the wild-type activity
E114K
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mutant enzyme with no esterase and reductase activity
G106N
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mutant enzyme with no esterase and reductase activity
G191D
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mutant enzyme reveals esterase, 105% of the wild-type activity, but no reductase activity
G44C/S105N/A326T
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mutant enzyme with no esterase and reductase activity
G7D
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mutant enzyme with no esterase and reductase activity
R314C
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mutant enzyme with no esterase and reductase activity
S145F
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mutant enzyme with no esterase and reductase activity
S22L/S164F
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mutant enzyme with no esterase and reductase activity
additional information
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N-terminal engineering of glutamyl-tRNA reductase with positive charge arginine to increase 5-aminolevulinic acid biosynthesis. Insertion of lysine or arginine residues (especially one arginine residue) behind Thr2 of GluTR significantly increased the stability of GluTR. By co-expression of this GluTR variant R1 and the glutamate-1-semialdehyde aminotransferase, 5-aminolevulinic acid production is improved 1.76fold to 1220 mg/L
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-80°C, 6*His-tagged enzyme is stable for at least 6 months
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wild-type GluTR and variants
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wild-type GluTR and variants produced as N-terminal His6-fusion proteins
expression plasmid pBKCwt overexpression of a 6*His-tagged enzyme
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overexpression in Escherichia coli
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synthesis
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the recombinant engineered GluTR variant R1 can be used for improvement of the C5 pathway to enhance 5-aminolevulinic acid and other products
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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
J. Biol. Chem.
277
48657-48663
2002
Escherichia coli
brenda
Randau, L.; Schauer, S.; Ambrogelly, A.; Salazar, J.C.; Moser, J.; Sekine, S.; Yokoyama, S.; Soll, D.; Jahn, D.
tRNA recognition by glutamyl-tRNA reductase
J. Biol. Chem.
279
34931-34937
2004
Escherichia coli
brenda
Schauer, S.; Luer, C.; Moser, J.
Large scale production of biologically active Escherichia coli glutamyl-tRNA reductase from inclusion bodies
Protein Expr. Purif.
31
271-275
2003
Escherichia coli
brenda
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
FEBS J.
274
4609-4614
2007
Escherichia coli (P0A6X1), Escherichia coli
brenda
Zhang, J.; Weng, H.; Ding, W.; Kang, Z.
N-terminal engineering of glutamyl-tRNA reductase with positive charge arginine to increase 5-aminolevulinic acid biosynthesis
Bioengineered
8
424-427
2017
Escherichia coli
brenda