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Literature summary for 6.1.1.17 extracted from

  • Katz, A.; Banerjee, R.; de Armas, M.; Ibba, M.; Orellana, O.
    Redox status affects the catalytic activity of glutamyl-tRNA synthetase (2010), Biochem. Biophys. Res. Commun., 398, 51-55.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.17

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of GST-GluRS1 Acidithiobacillus ferrooxidans

Inhibitors

Inhibitors Comment Organism Structure
H2O2 GluRS1 activity is reversibly inactivated upon oxidation by hydrogen peroxide, the enzyme loses 90% activity after 10 min at 0.3 mM H2O2. tRNAGlu is able to protect GluRS1 against oxidative inactivation by hemin plus hydrogen peroxide. GluRS1 is the main enzyme responsible for supplying Glu-tRNAGlu for heme biosynthesis. Partial recovery of the enzymatic activity by treatment with DTT or 2-mercaptoethanol Acidithiobacillus ferrooxidans
hemin GluRS1 activity is reversibly inactivated upon oxidation by hemin. tRNAGlu is able to protect GluRS1 against oxidative inactivation by hemin plus hydrogen peroxide Acidithiobacillus ferrooxidans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Acidithiobacillus ferrooxidans
Zn2+ bound at the active site, Zn2+ is essential for the proper binding of glutamate to GluRS. GluRS1 contains one Zn2+ ion per enzyme molecule, determination of the Zn2+ content of GluRS1 by mass spectrometry, overview. A relatively canonical SWIM motif, C-X-C-X24-C-X-E, forms a Zn2+-binding site Acidithiobacillus ferrooxidans

Organism

Organism UniProt Comment Textmining
Acidithiobacillus ferrooxidans
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-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-GluRS1 by glutathione affinity chromatography, followed by removal of GST Acidithiobacillus ferrooxidans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information discriminating GluRS specifically aminoacylates tRNAGlu with glutamate. Acidithiobacillus ferrooxidans GluRS1 contains cysteines 98, 100 and 125 together with glutamate 127 clustered in the catalytic domain Acidithiobacillus ferrooxidans ?
-
 ?

Subunits

Subunits Comment Organism
More Acidithiobacillus ferrooxidans GluRS1 contains cysteines 98, 100 and 125 together with glutamate 127 clustered in the catalytic domain Acidithiobacillus ferrooxidans

Synonyms

Synonyms Comment Organism
GluRS
-
 Acidithiobacillus ferrooxidans
GluRS1
-
 Acidithiobacillus ferrooxidans
Glutamyl-tRNA synthetase
-
 Acidithiobacillus ferrooxidans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Acidithiobacillus ferrooxidans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Acidithiobacillus ferrooxidans

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Acidithiobacillus ferrooxidans

General Information

General Information Comment Organism
metabolism the sensitivity to oxidation of GluRS1 might provide a means to regulate tetrapyrrole and protein biosynthesis in response to extreme changes in both the redox and heme status of the cell via a single enzyme. The glutamate moiety of Glu-tRNAGlu is transformed to glutamate semialdehyde by the glutamyl-tRNA reductase and is subsequently transformed to 4-aminolevulinic acid, the universal precursor of tetrapyrroles, by the glutamate semialdehyde amidotransferase Acidithiobacillus ferrooxidans
additional information targets for oxidation-based inhibition are cysteines from a SWIM zinc-binding motif located in the tRNA acceptor helix-binding domain. Oxidation of the metal-binding site cysteine of GluRS1 significantly impaired catalysis. Also, binding of ATP or tRNA protects the distant cysteines of the SWIM motif Acidithiobacillus ferrooxidans
physiological function in cells containing glutaminyl-tRNA synthetase, GlnRS, discriminating GluRS specifically aminoacylates tRNAGlu with glutamate. One of two GluRSs from the extremophile Acidithiobacillus ferrooxidans, is inactivated when intracellular heme is elevated suggesting a specific role for GluRS1 in the regulation of tetrapyrrole biosynthesis Acidithiobacillus ferrooxidans