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Information on EC 1.2.1.70 - glutamyl-tRNA reductase and Organism(s) Methanopyrus kandleri and UniProt Accession Q9UXR8

for references in articles please use BRENDA:EC1.2.1.70
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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.
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Methanopyrus kandleri
UNIPROT: Q9UXR8
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The taxonomic range for the selected organisms is: Methanopyrus kandleri
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
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-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
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
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-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
additional information
-
no significant stimulation by high salt concentrations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
1.0 mM, 90% inhibition
glutamate-1-semialdehyde
1.0 mM, 50% inhibition
glutamycin
2.5 mM, 75% inhibition
heme
0.007 mM, 70% inhibition
iodoacetamide
0.01 mM, 30% inhibition, 0.1 mM, complete inhibition
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
PtCl4
0.1 mM, 55% inhibition, 1.0 mM, 90% inhibition
ZnCl2
0.2 mM, 45% inhibition, 5.0 mM, 90% inhibition
5,5'-dithiobis-(2-nitrobenzoic acid)
-
-
glutamycin
-
competitive
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
190000
gel filtration
45436
x * 45436, electrospray ionization mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45436, electrospray ionization mass spectrometry
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
C48S
90% of the GluTR reductase activity compared to wild-type enzyme, 95% of the GluTR esterase activity compared to wild-type enzyme
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
C48S
-
complete loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
overexpression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moser, J.; Schubert, W.D.; Heinz, D.W.; Jahn, D.
Structure and function of glutamyl-tRNA reductase involved in 5-aminolaevulinic acid formation
Biochem. Soc. Trans.
30
579-584
2002
Methanopyrus kandleri
Manually annotated by BRENDA team
Moser, J.; Lorenz, S.; Hubschwerlen, C.; Rompf, A.; Jahn, D.
Methanopyrus kandleri glutamyl-tRNA reductase
J. Biol. Chem.
274
30679-30685
1999
Methanopyrus kandleri (Q9UXR8), Methanopyrus kandleri
Manually annotated by BRENDA team
Schubert, W.D.; Moser, J.; Schauer, S.; Heinz, D.W.; Jahn, D.
Structure and function of glutamyl-tRNA reductase, the first enzyme of tetrapyrrole biosynthesis in plants and prokaryotes
Photosynth. Res.
74
205-215 (c)
2002
Methanopyrus kandleri
Manually annotated by BRENDA team