BRENDA - Enzyme Database

Effect of hydrogen peroxide on the biosynthesis of heme and proteins potential implications for the partitioning of Glu-tRNA(Glu) between these pathways

Farah, C.; Levican, G.; Ibba, M.; Orellana, O.; Int. J. Mol. Sci. 15, 23011-23023 (2014)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
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
Commentary
Organism
1.2.1.70
recombinant overexpression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Acidithiobacillus ferrooxidans
Inhibitors
EC Number
Inhibitors
Commentary
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
Commentary
Organism
Structure
1.2.1.70
Mg2+
required
Acidithiobacillus ferrooxidans
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
Acidithiobacillus ferrooxidans
-
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.70
Acidithiobacillus ferrooxidans
B7J8J0
-
-
Purification (Commentary)
EC Number
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
742701
Acidithiobacillus ferrooxidans
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
Temperature Optimum [C]
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
1.2.1.70
37
-
assay at
Acidithiobacillus ferrooxidans
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.2.1.70
7.2
-
assay at
Acidithiobacillus ferrooxidans
Cofactor
EC Number
Cofactor
Commentary
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
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
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) (protein specific)
EC Number
Commentary
Organism
1.2.1.70
recombinant overexpression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Acidithiobacillus ferrooxidans
Cofactor (protein specific)
EC Number
Cofactor
Commentary
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
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
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 (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.2.1.70
Mg2+
required
Acidithiobacillus ferrooxidans
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
Acidithiobacillus ferrooxidans
-
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
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) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
742701
Acidithiobacillus ferrooxidans
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
Temperature Optimum [C] (protein specific)
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
1.2.1.70
37
-
assay at
Acidithiobacillus ferrooxidans
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.2.1.70
7.2
-
assay at
Acidithiobacillus ferrooxidans
General Information
EC Number
General Information
Commentary
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
General Information (protein specific)
EC Number
General Information
Commentary
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