Literature summary extracted from
Farah, C.; Levican, G.; Ibba, M.; Orellana, O.
Effect of hydrogen peroxide on the biosynthesis of heme and proteins potential implications for the partitioning of Glu-tRNA(Glu) between these pathways (2014), Int. J. Mol. Sci., 15, 23011-23023 .
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.2.1.70 |
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 |
Acidithiobacillus ferrooxidans |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.2.1.70 |
recombinant overexpression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) |
Acidithiobacillus ferrooxidans |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.2.1.70 |
H2O2 |
inactivates the enzyme. H2O2 decreases the stimulation of GluTR by glutamate semialdehyde 1-2 aminomutase, GSAM |
Acidithiobacillus ferrooxidans |
|
1.2.1.70 |
heme |
feedback inhibition |
Acidithiobacillus ferrooxidans |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.2.1.70 |
Mg2+ |
required |
Acidithiobacillus ferrooxidans |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.2.1.70 |
L-glutamyl-tRNAGlu + NADPH + H+ |
Acidithiobacillus ferrooxidans |
- |
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.2.1.70 |
Acidithiobacillus ferrooxidans |
B7J8J0 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.2.1.70 |
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography |
Acidithiobacillus ferrooxidans |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.2.1.70 |
L-glutamyl-tRNAGlu + NADPH + H+ |
- |
Acidithiobacillus ferrooxidans |
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.2.1.70 |
GluTR |
- |
Acidithiobacillus ferrooxidans |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.2.1.70 |
37 |
- |
assay at |
Acidithiobacillus ferrooxidans |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.2.1.70 |
7.2 |
- |
assay at |
Acidithiobacillus ferrooxidans |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.2.1.70 |
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) |
Acidithiobacillus ferrooxidans |
|
1.2.1.70 |
NADP+ |
- |
Acidithiobacillus ferrooxidans |
|
1.2.1.70 |
NADPH |
- |
Acidithiobacillus ferrooxidans |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.2.1.70 |
metabolism |
glutamyl-tRNA reductase (GluTR) is the key enzyme for heme biosynthesis. The flow of glutamyl-tRNA is diverted from heme biosynthesis towards protein synthesis under oxidative stress conditions. In the C5 pathway, 5-aminolevulinic acid is synthesized from Glu-tRNAGlu in two steps. First, the glutamate moiety of Glu-tRNAGlu is reduced to glutamate semialdehyde (GSA) by glutamyl-tRNA reductase (GluTR), and then GSA is converted to 5-aminolevulinic acid by the glutamate semialdehyde 1-2 aminomutase (GSAM) |
Acidithiobacillus ferrooxidans |
1.2.1.70 |
physiological function |
in chemolithoautotrophic bacteria like Acidithiobacillus ferrooxidans that use the C5 pathway to synthesize tetrapyrroles, high demand for Glu-tRNAGlu for heme biosynthesis is expected, due to the high cytochrome content required for respiration using poor electron donors, such as ferrous ions. This bacterium has a complex system of glutamyl-tRNA formation composed of two non-discriminating glutamyl-tRNA synthetases (GluRS1 and GluRS2) and up to four tRNAGlu isoacceptors, with GluRS1 serving as the main enzyme for Glu-tRNAGlu formation. Three out of four glutamyl-tRNAs can act as donors for both heme and protein synthesis, while the fourth is not a substrate of GluTR and likely acts exclusively in protein synthesis |
Acidithiobacillus ferrooxidans |