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Information on EC 1.2.1.70 - glutamyl-tRNA reductase and Organism(s) Escherichia coli and UniProt Accession P0A6X1

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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.
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Escherichia coli
UNIPROT: P0A6X1
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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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutamate tRNA reductase
-
-
glutamate-specific tRNA reductase
-
-
glutamyl transfer RNA reductase
-
-
glutamyl-tRNA reductase
-
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reductase, glutamyl-transfer ribonucleate
-
-
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
119940-26-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutaminyl-tRNAGlu + NADPH + H+
? + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
restores activity after treatment with chelating agents
Mg2+
-
stimulates, restores activity after treatment with chelating agents
Mn2+
-
restores activity after treatment with chelating agents
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
5 mM, 25% inhibition
2,2'-dipyridyl
-
5 mM, 20% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
-
1 mM, 80% inhibition
EDTA
-
10 mM, 55% inhibition
EGTA
-
10 mM, 35% inhibition
glutamycin
-
3 mM, 90% inhibition
heme
-
feedback inhibition
iodoacetamide
-
0.1 mM, complete inhibition
PtCl4
-
1 mM, 90% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
L-glutamyl-tRNAGlu
-
pH 8.1, 37°C
0.039
NADPH
-
pH 8.1, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13
L-glutamyl-tRNAGlu
-
pH 8.1, 37°C
0.15
NADPH
-
pH 8.1, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
-
gel filtration
48000
-
2 * 48000, homodimer with an extended structure, SDS-PAGE
48448
-
2 * 48448, homodimer with an extended structure, electrospray ionization mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
mutant enzyme with esterase activity 95% of the wild-type activity and reductase activity with 90% of the wild-type activity
C50S
-
mutant enzyme with no esterase and reductase activity
C74S
-
mutant enzyme with esterase activity 110% of the wild-type activity and reductase activity with 120% of the wild-type activity
E114K
-
mutant enzyme with no esterase and reductase activity
G106N
-
mutant enzyme with no esterase and reductase activity
G191D
-
mutant enzyme reveals esterase, 105% of the wild-type activity, but no reductase activity
G44C/S105N/A326T
-
mutant enzyme with no esterase and reductase activity
G7D
-
mutant enzyme with no esterase and reductase activity
R314C
-
mutant enzyme with no esterase and reductase activity
S145F
-
mutant enzyme with no esterase and reductase activity
S22L/S164F
-
mutant enzyme with no esterase and reductase activity
additional information
-
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 6*His-tagged enzyme is stable for at least 6 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type GluTR and variants
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type GluTR and variants produced as N-terminal His6-fusion proteins
expression plasmid pBKCwt overexpression of a 6*His-tagged enzyme
-
overexpression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
the recombinant engineered GluTR variant R1 can be used for improvement of the C5 pathway to enhance 5-aminolevulinic acid and other products
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team