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
1.2.1.70
-
RECOMMENDED NAME
GeneOntology No.
glutamyl-tRNA reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu = L-glutamyl-tRNAGlu + NADPH + H+
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Porphyrin and chlorophyll metabolism
-
tetrapyrrole biosynthesis I (from glutamate)
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glutamate tRNA reductase
-
-
glutamate-specific tRNA reductase
-
-
glutamyl transfer RNA reductase
-
-
glutamyl-tRNA reductase
-
-
glutamyl-tRNA reductase
-
-
glutamyl-tRNA reductase
-
-
glutamyl-tRNA reductase
-
-
glutamyl-tRNA reductase
-
-
glutamyl-tRNA reductase
P28462
-
glutamyl-tRNA reductase
-
-
glutamyl-tRNA reductase
Streptomyces coelicolor J1501
-
-
-
glutamyl-tRNA reductase
-
-
GluTR
P0A6X1
-
GluTR
-
-
GluTR
-
-
GluTR
D3JIR5
-
GluTR
Streptomyces coelicolor J1501
-
-
-
reductase, glutamyl-transfer ribonucleate
-
-
CAS REGISTRY NUMBER
COMMENTARY
119940-26-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain CC-124
Uniprot
Manually annotated by BRENDA team
Chlamydomonas reinhardtii CC-124
strain CC-124
Uniprot
Manually annotated by BRENDA team
L. cv. Aonagajibai
-
-
Manually annotated by BRENDA team
; mutant albostrians
-
-
Manually annotated by BRENDA team
cultivar Svalöf Bonus
-
-
Manually annotated by BRENDA team
Norway spruce
UniProt
Manually annotated by BRENDA team
strain J1501
-
-
Manually annotated by BRENDA team
Streptomyces coelicolor J1501
strain J1501
-
-
Manually annotated by BRENDA team
subspecies asukaensis
-
-
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
GluTR is the first enzyme committed to tetrapyrrole biosynthesis by the C5-pathway
metabolism
-
GluTR is the first committed enzyme of plant 5-aminolevulinic acid synthesis and 5-aminolevulinic acid synthesis has been shown to be the rate limiting step of tetrapyrrole biosynthesis
metabolism
-
GluTR is proposed to be the key regulatory enzyme of tetrapyrrole biosynthetic pathway that is tightly controlled at transcriptional and posttranslational levels
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutaminyl-tRNAGlu + NADPH + H+
? + NADP+ + tRNAGlu
show the reaction diagram
P0A6X1
-
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
show the reaction diagram
P28462
-
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
show the reaction diagram
-
much higher activity occurs with NADPH than with NADH
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
show the reaction diagram
-
Acidithiobacillus ferrooxidans contains three tRNAGlu where only 2 are a substrate for glutamyl-tRNA reductase
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
show the reaction diagram
Q9FPR7
the enzyme also exhibits an esterase activity
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
-
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
-
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
P0A6X1
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
D3JIR5, -
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
complex formation between glutamyl-tRNA synthetase and glutamyl-tRNA reductase during the tRNA-dependent synthesis of 5-aminolevulinic acid
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
glutamyl-tRNA reductase is the solely light-regulated enzyme of 5-aminolevulinic acid-synthesis system, and the elevation of glutamate by light may contribute to the stimulation of 5-aminolevulinic acid synthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
stimulation of the synthesis of 5-aminolevulinic acid by benzyladenine is caused by increased levels of glutamyl-tRNA reductase and that the reductase is the regulatory and rate-determining enzyme in the 5-aminolevulinic-synthesis system except in untreated etioplasts, in which the level of glutamyl-tRNA may be rate-determining factor
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
Q42843
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme directs glutamate to chlorophyll biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme is involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme is involved in the C5 pathway
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
A7-U66, U29-A41, A53-U61 and U72 are expected to be required for recognition by the barley chloroplast glutamyl-tRNA(Glu) reductase
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-, Q9UXR8
in absence of NADPH, an esterase activity of GluTR hydrolyzes the highly reactive thioester of tRNAGlu to release glutamate
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
in presence of NADPH, the end product, glutamate-1-semialdehyde is formed. In the absence of NADPH, Escherichia coli GluTR exhibits substrate esterase activity
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
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
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
Q42843
the fusion protein with glutathione S-transferase uses tRNAGlu from Hordeum vulgare chloroplast preferentially to Escherichia coli tRNAGlu
-
-
?
additional information
?
-
-
formation of 5-aminolevulinic acid in 5-week-old AtHEMA1-expressing tobacco plants grown in continuous light could be shown to be significantly altered but does not result in significant changes of the amounts of tetrapyrrole intermediates, chlorophyll or heme
-
-
?
additional information
?
-
-
hemA with Lys insertion overexpressing Escherichia coli strain shows an increased 5-aminolevulinic acid accumulation indicating that the reduction of glutamyl-tRNA to glutamate-1-semialdehyde is a rate-limiting step
-
-
?
additional information
?
-
-
identification of a GluTR binding protein, GluTRBP, that is localized in chloroplasts and is part of a 300000 Da protein complex in the thylakoid membrane, protein does not modulate activity of ALA synthesis, but the knockout of GluTRBP is lethal in Arabidopsis thaliana, whereas mutants expressing reduced levels of GluTRBP contain less heme
-
-
?
additional information
?
-
-
up to 7fold increased GluTR content in adult transgenic Arabidopsis plants two days after ethanol application but there is no significant increase in 5-aminolevulinic acid synthesis rates in comparison to ethanol-treated wild-type plants
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
D3JIR5, -
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
complex formation between glutamyl-tRNA synthetase and glutamyl-tRNA reductase during the tRNA-dependent synthesis of 5-aminolevulinic acid
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
glutamyl-tRNA reductase is the solely light-regulated enzyme of 5-aminolevulinic acid-synthesis system, and the elevation of glutamate by light may contribute to the stimulation of 5-aminolevulinic acid synthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
stimulation of the synthesis of 5-aminolevulinic acid by benzyladenine is caused by increased levels of glutamyl-tRNA reductase and that the reductase is the regulatory and rate-determining enzyme in the 5-aminolevulinic-synthesis system except in untreated etioplasts, in which the level of glutamyl-tRNA may be rate-determining factor
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
Q42843
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme directs glutamate to chlorophyll biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme is involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
the enzyme is involved in the C5 pathway
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
heme
Q42843
the fusion protein with glutathione S-transferase contains heme, which can be reduced by NADPH and oxidized by air
heme
P28462
one molecule per glutamyl-tRNA reductase molecule
heme
-
the levels of GluTR are regulated by the heme status
NADH
-
much higher activity occurs with NADPH than with NADH
NADPH
-
half-maximal rate at 0.005 mM, saturation is not reached even at 10 mM NADH
heme
-
enzyme shows Soret peak at 420 nm and a broad absorbance around 540 nm, data suggest that heme is bound preferentially to the dimeric form of GluTR
additional information
-, Q9UXR8
the enzyme does not possess a chromophoric prosthetic group
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
additional information
-
no significant stimulation by high salt concentrations
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
5 mM, 25% inhibition
2,2'-dipyridyl
-
5 mM, 20% inhibition
2,4-diphenyl-6-styryl-1-p-tolyl-pyridinium boron tetrafluoride
-
IC50: 0.01 mM
4-[4-(3,4-dihydroxyphenyl)-2,3-dimethylbutyl]benzene-1,2-diol
-
IC50: 0.055 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-, Q9UXR8
1.0 mM, 90% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
-
1 mM, 80% inhibition
5,5'-dithiobis-(2-nitrobenzoic acid)
-
-
5,6-dichloro-1,3-benzodioxol-2-one
-
IC50: 0.055 mM
Cd2+
-
1 mM Cd(Ac)2, 92% inhibition
Co2+
-
10 mM CoCl2, 78% inhibition
Cu2+
-
1 mM CuCl2, 84% inhibition
EDTA
-
10 mM, 55% inhibition
EGTA
-
10 mM, 35% inhibition
Fe2+
-
5 mM FeSO4, 66% inhibition
-
Fe3+
-
10 mM FeCl3, 80% inhibition
-
glutamate 1-semialdehyde
-
0.2 mM, 50% inhibition
glutamate-1-semialdehyde
-, Q9UXR8
1.0 mM, 50% inhibition
glutamycin
-
competitive
glutamycin
-, Q9UXR8
2.5 mM, 75% inhibition
glutamycin
-
3 mM, 90% inhibition
heme
-
0.004 mM, 50% inhibition
heme
-
0.05 mM, 50% inhibition
heme
-, Q9UXR8
0.007 mM, 70% inhibition
heme
-
0.002 mM, 63% inhibition of non-truncated enzyme
heme
Q9FPR7
80% inhibition at 0.005 mM
heme
-
when intracellular heme is in excess, the cells respond by a dramatic decrease of the level of GluTR
Hemin
Q42843
50% inhibition at 0.0015 mM
iodoacetamide
-, Q9UXR8
0.01 mM, 30% inhibition, 0.1 mM, complete inhibition
iodoacetamide
-
0.1 mM, complete inhibition
N-tosyl-L-phenylalaninechloromethyl ketone
-, Q9UXR8
0.1 mM, 90% inhibition, 1.0 mM, complete inhibition
PbCl2
-, Q9UXR8
0.1 mM, 60% inhibition, 1.0 mM, complete inhibition
PtCl4
-, Q9UXR8
0.1 mM, 55% inhibition, 1.0 mM, 90% inhibition
PtCl4
-
1 mM, 90% inhibition
Zn2+
-
2.5 mM, ZnSO4, 94% inhibition
ZnCl2
-, Q9UXR8
0.2 mM, 45% inhibition, 5.0 mM, 90% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
glutamate-1-semialdehyde aminotransferase
P28462
2.5fold activity in presence of glutamate-1-semialdehyde aminotransferase
-
glutamate-1-semialdehyde aminotransferase
-
2.5fold activity in presence of glutamate-1-semialdehyde aminotransferase
-
Ozone
-
induces expression in photosynthetic tissues
heme
-
under high heme requirement for respiration levels of GluTR increase
additional information
-
is induced in photosynthetic tissues by oxidative stresses such as wounding
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.024
-
L-glutamyl-tRNAGlu
-
pH 8.1, 37°C
0.039
-
NADPH
-
pH 8.1, 37°C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.15
-
NADPH
-
pH 8.1, 37°C
0.13
-
L-glutamyl-tRNAGlu
-
pH 8.1, 37°C
additional information
-
additional information
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01
-
2,4-diphenyl-6-styryl-1-p-tolyl-pyridinium boron tetrafluoride
-
IC50: 0.01 mM
0.055
-
4-[4-(3,4-dihydroxyphenyl)-2,3-dimethylbutyl]benzene-1,2-diol
-
IC50: 0.055 mM
0.055
-
5,6-dichloro-1,3-benzodioxol-2-one
-
IC50: 0.055 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.12
-
Q42843
fusion protein with glutathione S-transferase
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.1
-
-, Q9UXR8
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-, Q9UXR8
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Streptomyces coelicolor J1501
-
-
-
Manually annotated by BRENDA team
-
kinetin but not cytokinin stimulates expression of glutamyl-tRNA reductase expression in etiolated plants
Manually annotated by BRENDA team
-
kinetin stimulates expression of glutamyl-tRNA reductase in etiolated seedlings
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
stroma of greening chloroplast
Manually annotated by BRENDA team
-
glutamyl-tRNA reductase protein is 2fold more abundant in light grown cells compared to dark grown cells
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
49000
-
P28462
SDS-PAGE, recombinant protein
50000
-
-
SDS–PAGE of His6-tagged GluTR
50490
-
-
MALDI-TOF mass spectrometry of His6-tagged GluTR
52500
-
Q9FPR7
deduced from sequence
101000
-
-
sucrose density gradient sedimentation, dimer
104000
-
-
cross-linking of GluTR with glutaraldehyde
130000
-
-
glycerol gradient sedimentation, gel filtration
148000
-
-
relative molecular mass of native recombinant GluTR after removal of His6-tag, determined by gel permeation chromatography
180000
-
-
gel filtration
190000
-
-, Q9UXR8
gel filtration
250000
-
Q42843
gel filtration
270000
-
-
gel filtration
350000
-
-
glycerol density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 54000, SDS-PAGE
?
-
x * 39000, SDS-PAGE
?
-, Q9UXR8
x * 45436, electrospray ionization mass spectrometry
dimer
-
2 * 48000, homodimer with an extended structure, SDS-PAGE; 2 * 48448, homodimer with an extended structure, electrospray ionization mass spectrometry
dimer
P28462
2 * 49000, gel-filtration in presence of 5% glycerol
dimer
-
2 * 52500, sucrose gradient sedimentation compared to calculation from sequence
heterotetramer
-
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
Q9FPR7
2 * 52500, gel filtration
homodimer
-
2 * 50000, probably enyzme has an overall V shape that makes the protein migrate slower in gel permeation chromatography
monomer
-
1 * 130000, SDS-PAGE
monomer
P28462
1 * 49000, gel-filtration without glycerol
tetramer
Q42843
4 * 60000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80°C, 6*His-tagged enzyme is stable for at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by Ni2+-Sepharose affinity chromatography to near homogeneity
-
Ni-affinity chromatography
-
Ni-affinity chromatography
-
wild-type GluTR and variants
P0A6X1
fusion protein with glutathione S-transferase
Q42843
Ni-affinity chromatography
P28462
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli BL21
-
His(6)-GluTR overexpressed in Escherichia coli BL21 (DE3)
-
N-terminal His6-tagged GluTR expressed in Escherichia coli
-
AtHemA1 overexpression in Nicotiana tabacum cv Samsun NN using Agrobacterium tumefaciens and Arabidopsis thaliana by transformation
-
expression as His-tag fusion protein in Escherichia coli
Q9FPR7
expression in Escherichia coli
-
expression plasmid pBKCwt overexpression of a 6*His-tagged enzyme
-
overexpression in Escherichia coli
-
wild-type GluTR and variants produced as N-terminal His6-fusion proteins
P0A6X1
expression in Escherichia coli as a fusion protein with glutathione S-transferase
Q42843
overexpression in Escherichia coli
-
expression in Escherichia coli
P28462
hemA ligated into pUC19 vector with a Lys insert between Thr-2 and Leu-3 at N terminus, overexpression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression profiles in the first hours of deetiolation of Arabidopsis seedlings show an abundance of GluTR that gradually increased with chlorophyll biosynthesis
-
etiolation of initially green dark-grown larch cotyledons is connected with decreasing content of glutamyl-tRNA reductase
-
the relative amount of GluTR is similar both in the dark-grown and light/dark-grown gabaculine-treated seedlings
D3JIR5
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C48A
-
no 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
C50S
P0A6X1
inactive
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
E54K
P0A6X1
retains 6% reductase and 2% esterase 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
H99N
P0A6X1
retains 5% reductase and 4% esterase activity
Q116L
P0A6X1
lacks reductase activity whereas 30% esterase activity is retained
R314C
-
mutant enzyme with no esterase and reductase activity
R52K
P0A6X1
retains 5% reductase and 4% esterase activity
R52Q
P0A6X1
inactive
S109A
P0A6X1
retains 28% reductase and 30% esterase activity
S145F
-
mutant enzyme with no esterase and reductase activity
S22L/S164F
-
mutant enzyme with no esterase and reductase activity
T49V
P0A6X1
retains 10% reductase and 5% esterase activity
I318L/R322G/N454D
-
mutant enzyme with greatly reduced activity
I464P
-
mutant enzyme with greatly reduced activity
L387H/L302S
-
mutant enzyme with greatly reduced activity
C393S
-, Q9UXR8
95% of the GluTR reductase activity compared to wild-type enzyme, 100% of the GluTR esterase activity compared to wild-type enzyme
C42S
-, Q9UXR8
no GluTR reductase and GluTR esterase activity
C48S
-
complete loss of activity
C48S
-, Q9UXR8
90% of the GluTR reductase activity compared to wild-type enzyme, 95% of the GluTR esterase activity compared to wild-type enzyme
C6S
-, Q9UXR8
130% of the GluTR reductase activity compared to wild-type enzyme, 120% of the GluTR esterase activity compared to wild-type enzyme
C90S
-, Q9UXR8
85% of the GluTR reductase activity compared to wild-type enzyme, 105% of the GluTR esterase activity compared to wild-type enzyme
H84A
-, Q9UXR8
no GluTR reductase activity, 5% of the GluTR esterase activity compared to wild-type enzyme
additional information
-
insertional knockout mutants show heme contents of the roots about half of that of the wild-type and reduction of the ozone-induced increase in heme content
additional information
-
as excessive accumulation of GluTR in transgenic plants does not correlate with increased 5-aminolevulinic acid formation, it is hypothesized that 5-aminolevulinic acid synthesis is additionally limited by other effectors that balance the allocation of 5-aminolevulinic acid with the activity of enzymes of chlorophyll and heme biosynthesis
M122K/K154N/F371L/E400K
-
mutant enzyme with greatly reduced activity
additional information
-
a 30 amino acid N-terminal deletion has no detrimental effect on the catalytic activity of the enzyme
H84N
-, Q9UXR8
30% of the GluTR reductase activity compared to wild-type enzyme, 15% of the GluTR esterase activity compared to wild-type enzyme
additional information
-
the knockout mutant is absolutely dependent on supplementation with 5-aminolevulinic acid
additional information
Streptomyces coelicolor J1501
-
the knockout mutant is absolutely dependent on supplementation with 5-aminolevulinic acid
-
additional information
-
the knockout mutant is absolutely dependent on supplementation with 5-aminolevulinic acid
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
recombinant Escherichia coli allows efficient production of 5-aminolevulinic acid directly from glucose
additional information
-
the function of GluTR is regulated by mechanisms that involve the steady-state level of the protein or the activity of the enzyme in response to the cellular heme status
additional information
-
the tetrapyrrole biosynthetic pathway is controlled by HEMA2 and FC1, which normally functions for heme biosynthesis in nonphotosynthetic tissues, but is induced in photosynthetic tissues under oxidative conditions to supply heme for defensive hemoproteins outside plastids