Information on EC 1.2.1.70 - glutamyl-tRNA reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.2.1.70
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RECOMMENDED NAME
GeneOntology No.
glutamyl-tRNA reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu = L-glutamyl-tRNAGlu + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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heme metabolism
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Metabolic pathways
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Porphyrin and chlorophyll metabolism
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tetrapyrrole biosynthesis I (from glutamate)
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CC-124
Uniprot
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain J1501
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Manually annotated by BRENDA team
strain J1501
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Manually annotated by BRENDA team
subspecies asukaensis
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Manually annotated by BRENDA team
PCC 6803
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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
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?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
show the reaction diagram
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
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no significant stimulation by high salt concentrations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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5 mM, 25% inhibition
2,2'-dipyridyl
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5 mM, 20% inhibition
2,4-diphenyl-6-styryl-1-p-tolyl-pyridinium boron tetrafluoride
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IC50: 0.01 mM
4-[4-(3,4-dihydroxyphenyl)-2,3-dimethylbutyl]benzene-1,2-diol
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IC50: 0.055 mM
5,5'-dithiobis(2-nitrobenzoic acid)
5,5'-dithiobis-(2-nitrobenzoic acid)
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5,6-dichloro-1,3-benzodioxol-2-one
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IC50: 0.055 mM
Cd2+
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1 mM Cd(Ac)2, 92% inhibition
Cu2+
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1 mM CuCl2, 84% inhibition
EDTA
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10 mM, 55% inhibition
EGTA
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10 mM, 35% inhibition
Fe2+
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5 mM FeSO4, 66% inhibition
Fe3+
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10 mM FeCl3, 80% inhibition
glutamate 1-semialdehyde
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0.2 mM, 50% inhibition
glutamate-1-semialdehyde
1.0 mM, 50% inhibition
glutamycin
Hemin
50% inhibition at 0.0015 mM
iodoacetamide
N-tosyl-L-phenylalaninechloromethyl ketone
0.1 mM, 90% inhibition, 1.0 mM, complete inhibition
PbCl2
0.1 mM, 60% inhibition, 1.0 mM, complete inhibition
Zn2+
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2.5 mM, ZnSO4, 94% inhibition
ZnCl2
0.2 mM, 45% inhibition, 5.0 mM, 90% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cycloheximide
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glutamate-1-semialdehyde aminotransferase
heme
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under high heme requirement for respiration levels of GluTR increase
Ozone
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induces expression in photosynthetic tissues
additional information
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is induced in photosynthetic tissues by oxidative stresses such as wounding
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13
L-glutamyl-tRNAGlu
Escherichia coli
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pH 8.1, 37°C
0.15
NADPH
Escherichia coli
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pH 8.1, 37°C
additional information
additional information
Synechocystis sp.
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
2,4-diphenyl-6-styryl-1-p-tolyl-pyridinium boron tetrafluoride
Arabidopsis thaliana
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IC50: 0.01 mM
0.055
4-[4-(3,4-dihydroxyphenyl)-2,3-dimethylbutyl]benzene-1,2-diol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.12
fusion protein with glutathione S-transferase
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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kinetin but not cytokinin stimulates expression of glutamyl-tRNA reductase expression in etiolated plants
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
SDS-PAGE, recombinant protein
50000
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SDS–PAGE of His6-tagged GluTR
50490
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MALDI-TOF mass spectrometry of His6-tagged GluTR
52500
deduced from sequence
101000
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sucrose density gradient sedimentation, dimer
104000
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cross-linking of GluTR with glutaraldehyde
130000
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glycerol gradient sedimentation, gel filtration
148000
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relative molecular mass of native recombinant GluTR after removal of His6-tag, determined by gel permeation chromatography
180000
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gel filtration
190000
gel filtration
250000
gel filtration
270000
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gel filtration
350000
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glycerol density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
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2 * 52500 + 2 * 46000, sucrose gradient sedimentation of glutamyl-tRNA reductase preincubated with glutamate-1-semialdehyde aminotransferase. Both enzyme also co-precipitate in immunoprecipitation experiments
homodimer
monomer
tetramer
4 * 60000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized in presence of glutamycin, the structure is solved by the multiple isomorphous replacement method using three heavy atom derivatives. The structure is subsequently refined at a resolution of 1.95 A
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 6*His-tagged enzyme is stable for at least 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by Ni2+-Sepharose affinity chromatography to near homogeneity
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fusion protein with glutathione S-transferase
Ni-affinity chromatography
wild-type GluTR and variants
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AtHemA1 overexpression in Nicotiana tabacum cv Samsun NN using Agrobacterium tumefaciens and Arabidopsis thaliana by transformation
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expression as His-tag fusion protein in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli as a fusion protein with glutathione S-transferase
expression in Escherichia coli BL21
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expression plasmid pBKCwt overexpression of a 6*His-tagged enzyme
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hemA ligated into pUC19 vector with a Lys insert between Thr-2 and Leu-3 at N terminus, overexpression in Escherichia coli
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His(6)-GluTR overexpressed in Escherichia coli BL21 (DE3)
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N-terminal His6-tagged GluTR expressed in Escherichia coli
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overexpression in Escherichia coli
wild-type GluTR and variants produced as N-terminal His6-fusion proteins
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
etiolation of initially green dark-grown larch cotyledons is connected with decreasing content of glutamyl-tRNA reductase
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expression profiles in the first hours of deetiolation of Arabidopsis seedlings show an abundance of GluTR that gradually increased with chlorophyll biosynthesis
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the relative amount of GluTR is similar both in the dark-grown and light/dark-grown gabaculine-treated seedlings
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C48A
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no 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
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
E54K
retains 6% reductase and 2% esterase 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
H99N
retains 5% reductase and 4% esterase activity
Q116L
lacks reductase activity whereas 30% esterase activity is retained
R314C
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mutant enzyme with no esterase and reductase activity
R52K
retains 5% reductase and 4% esterase activity
S109A
retains 28% reductase and 30% esterase 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
T49V
retains 10% reductase and 5% esterase activity
I318L/R322G/N454D
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mutant enzyme with greatly reduced activity
I464P
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mutant enzyme with greatly reduced activity
L387H/L302S
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mutant enzyme with greatly reduced activity
M122K/K154N/F371L/E400K
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mutant enzyme with greatly reduced activity
C393S
95% of the GluTR reductase activity compared to wild-type enzyme, 100% of the GluTR esterase activity compared to wild-type enzyme
C42S
no GluTR reductase and GluTR esterase activity
C6S
130% of the GluTR reductase activity compared to wild-type enzyme, 120% of the GluTR esterase activity compared to wild-type enzyme
C90S
85% of the GluTR reductase activity compared to wild-type enzyme, 105% of the GluTR esterase activity compared to wild-type enzyme
H84A
no GluTR reductase activity, 5% of the GluTR esterase activity compared to wild-type enzyme
H84N
30% of the GluTR reductase activity compared to wild-type enzyme, 15% of the GluTR esterase activity compared to wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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recombinant Escherichia coli allows efficient production of 5-aminolevulinic acid directly from glucose
additional information
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