Any feedback?
Information on EC 1.2.1.70 - glutamyl-tRNA reductase
for references in articles please use BRENDA:EC1.2.1.70Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.2.1.70 glutamyl-tRNA reductaseIUBMB 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.
Specify your search results
Word Map
- 1.2.1.70
- tetrapyrrole
-
chlorophyl
- ala
-
5-aminolevulinic
- heme
- glutamate-1-semialdehyde
- protochlorophyllide
-
delta-aminolevulinic
- 1-semialdehyde
-
de-etiolation
- chelatase
- mg-protoporphyrin
- glu-trna
-
trna-dependent
- kandleri
-
pchlide
- gun4
- glu-trnaglu
-
trna-bound
-
2,1-aminomutase
- biotechnology
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
glutamyl-trna reductase, glutr, hema1, hema2, glutr1, athema1, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.7.2.13
-
-
formerly, part transferred
-
glutamyl-tRNA reductase
GluTR
GTR
GtrR
hemA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu = L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
119940-26-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
-
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
-
-
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
the enzyme also exhibits an esterase activity
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
the enzyme also exhibits an esterase activity
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
-
-
-
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
-
much higher activity occurs with NADPH than with NADH
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
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
-
the enzyme is involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
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
-
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
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
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
-
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
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme directs glutamate to chlorophyll biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
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
the fusion protein with glutathione S-transferase uses tRNAGlu from Hordeum vulgare chloroplast preferentially to Escherichia coli tRNAGlu
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme is involved in the C5 pathway
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + 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
?
-
-
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
-
-
?
additional information
?
-
GluTR employs hydride transfer from NADPH to the thioester-bound glutamate to produce glutamate-1-semialdehyde. The close contact between the nicotinamide ring of NADPH and the nucleophile Cys144 allows the transfer of hydride from NADPH to the thioester-bound glutamate. Tunnel formation in the GluTR-GluBP complex for release of product L-glutamate 1-semialdehyde
-
-
?
additional information
?
-
-
GluTR employs hydride transfer from NADPH to the thioester-bound glutamate to produce glutamate-1-semialdehyde. The close contact between the nicotinamide ring of NADPH and the nucleophile Cys144 allows the transfer of hydride from NADPH to the thioester-bound glutamate. Tunnel formation in the GluTR-GluBP complex for release of product L-glutamate 1-semialdehyde
-
-
?
additional information
?
-
-
binding of heme to the GluTR-binding protein (GBP) inhibits interaction of GBP with the N-terminal regulatory domain of isoform GluTR1, thus making it accessible to the Clp protease
-
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
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
-
the enzyme is involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
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
-
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
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme directs glutamate to chlorophyll biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
the enzyme is involved in the C5 pathway
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
the fusion protein with glutathione S-transferase contains heme, which can be reduced by NADPH and oxidized by air
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
heme
enzyme preparations with one molecule of heme bound per four GluTR subunits (heme/protein ratio of 1/4) have an increased inactivation rate by H2O2 compared to enzymes with one heme per twelve GluTR subunits (heme/protein ratio of 1/12)
NADPH
-
half-maximal rate at 0.005 mM, saturation is not reached even at 10 mM NADH
NADPH
NADPH-binding model of GluTR by using the homologous structure of a NADP-binding domain
additional information
the enzyme does not possess a chromophoric prosthetic group
-
additional information
-
the enzyme does not possess a chromophoric prosthetic group
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
-
no significant stimulation by high salt concentrations
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
fluorescent in blue light
-
FLU, the protein mediates inactivation of the enzyme at the membrane
-
H2O2
inactivates the enzyme. H2O2 decreases the stimulation of GluTR by glutamate semialdehyde 1-2 aminomutase, GSAM
N-tosyl-L-phenylalaninechloromethyl ketone
0.1 mM, 90% inhibition, 1.0 mM, complete inhibition
protein GBP
a soluble GluTR-binding protein, enzyme binding structure, overview. the GluTR-GBP complex is stable and has a low apparent dissociation constant. Protein GBP is initially found in chloroplast stroma
-
additional information
structure analysis of the FLUTPR-GluTR-GBP ternary complex, overview. Three mechanisms for plant GluTR activity regulation: (i) the end-product feedback inhibition by heme, (ii) repression by a membrane protein FLUORESCENT (FLU), and (iii) formation of complex with a soluble GluTR-binding protein (GBP)
-
heme
-
when intracellular heme is in excess, the cells respond by a dramatic decrease of the level of GluTR
heme
feedback inhibition, GluTR activity can be inhibited by heme in a concentration-dependent way regardless of the presence of GluTR binding protein, GluBP
iodoacetamide
0.01 mM, 30% inhibition, 0.1 mM, complete inhibition
protein FLU
the non-canonical tetratricopeptide repeat (TPR) domain of fluorescent (FLU) mediates complex formation with glutamyl-tRNA reductase. Protein FLU negatively regulates glutamyl-tRNA reductase (GluTR) during chlorophyll biosynthesis. A 2:2 FLUTPR-GluTR complex is the functional unit for FLU-mediated GluTR regulation. Enzyme binding complex structure analysis from crystal structures, detailed overview
-
protein FLU
membrane protein FLUORESCENT, protein FLU directly interacts with GluTR's dimerization domain through its tetratricopepetide-repeat (TPR) domain. Enzyme binding structure, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GluBP regulator
the GluTR regulator, GluTR binding protein (GluBP), spatially organizes tetrapyrrole synthesis by distributing enzyme GluTR into different suborganellar locations. GluBP belongs to a heme-binding family involved in heme metabolism. Complex structure of GluTR-GluBP from Arabidopsis thaliana, overview. The dimeric GluBP binds symmetrically to the catalytic domains of the V-shaped GluTR dimer via its C-terminal domain. A substantial conformational change of the GluTR NADPH-binding domain is observed, confirming the postulated rotation of the NADPH-binding domain for hydride transfer from NADPH to the substrate. Arg146, guarding the door for metabolic channeling, adopts alternative conformations, which may represent steps involved in substrate recognition and product release. GluBP stimulates GluTR catalytic efficiency with an approximate 3fold increase of the 5-aminolevulinic acid formation rate. Tunnel formation in the GluTR-GluBP complex for release of product L-glutamate 1-semialdehyde. GluBP stimulates GluTR activity and regulates GSA release
-
heme
-
under high heme requirement for respiration levels of GluTR increase
protein GSAM
stimulation of GluTR by glutamate semialdehyde 1-2 aminomutase, GSAM. GluTR activity is stimulated upon formation ofa complex with protein GSAM. This effect is observed only when GluTR contained a heme/protein ratio of 1/12. GluTR activity and the stimulation of this enzyme by protein GSAM are reduced by treatment with H2O2
-
additional information
-
is induced in photosynthetic tissues by oxidative stresses such as wounding
-
glutamate-1-semialdehyde aminotransferase
-
2.5fold activity in presence of glutamate-1-semialdehyde aminotransferase
-
glutamate-1-semialdehyde aminotransferase
2.5fold activity in presence of glutamate-1-semialdehyde aminotransferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
2,4-diphenyl-6-styryl-1-p-tolyl-pyridinium boron tetrafluoride
Arabidopsis thaliana
-
IC50: 0.01 mM
0.055
4-[4-(3,4-dihydroxyphenyl)-2,3-dimethylbutyl]benzene-1,2-diol
Arabidopsis thaliana
-
IC50: 0.055 mM