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Literature summary for 6.1.1.17 extracted from

  • Levican, G.; Katz, A.; de Armas, M.; Nunez, H.; Orellana, O.
    Regulation of a glutamyl-tRNA synthetase by the heme status (2007), Proc. Natl. Acad. Sci. USA, 104, 3135-3140.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information under high heme requirement for respiration increased levels of GluRS occur Acidithiobacillus ferrooxidans

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of GST-tagged isozyme GluRS1 in Escherichia coli strain Bl21(DE3), co-expression with Glu-tRNA reductase Acidithiobacillus ferrooxidans

Inhibitors

Inhibitors Comment Organism Structure
amino levulinic acid indirect inhibition, growth of Acidithiobacillus ferrooxidans in aminolevulic acid inhibits the activity of GluRS1, the reduced activity of GluRS1 is the result of an interaction of the enzyme with heme or any other intermediate tetrrapyrrole, amino levulic acid added to the reaction mixture has no effect in the activity of GluRSs Acidithiobacillus ferrooxidans
heme indirect mechanism, when intracellular heme is in excess, the cells respond by a dramatic decrease of GluRS activity, heme or any other precursor tetrapyrrole is the intracellular effector that triggers this regulatory mechanism Acidithiobacillus ferrooxidans
hemin recombinant GluRS1 enzyme is inhibited in vitro by hemin, but NADPH restores its activity, GluRS2 is also inhibited by hemin to a similar extent as GluRS1 Acidithiobacillus ferrooxidans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics of isozymes GluRS1 and GluRS2 Acidithiobacillus ferrooxidans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Acidithiobacillus ferrooxidans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate + tRNAGlu Acidithiobacillus ferrooxidans glutamyl-tRNA, formed by Glu-tRNA synthetase, is a substrate for protein biosynthesis and tetrapyrrole formation by the C5 pathway AMP + diphosphate + L-glutamyl-tRNAGlu
-
?
additional information Acidithiobacillus ferrooxidans GluRS plays a major role in regulating the cellular level of heme, aminoacylation of tRNAGlu correlates with the demand of heme, a transcriptional mechanism might control the level of GluRS1 in cells grown in Fe2+, under growth conditions in which cells do not require Glu-tRNA, as precursor for heme biosynthesis, up to 85% of GluRS1 is dispensable, but no major detrimental effect in the cell growth is observed. Thus, GluRS2 and the remaining 15% of the activity of GluRS1 are sufficient to provide the Glu-tRNA substrates for protein synthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Acidithiobacillus ferrooxidans
-
strain ATCC 23270, two isozymes GluRS1 and GluRS2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information GluRS is substrate of DsbA, a protein involved in the restoration of the reduced state of cysteines in proteins upon oxidation Acidithiobacillus ferrooxidans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + tRNAGlu
-
Acidithiobacillus ferrooxidans AMP + diphosphate + L-glutamyl-tRNAGlu
-
?
ATP + L-glutamate + tRNAGlu glutamyl-tRNA, formed by Glu-tRNA synthetase, is a substrate for protein biosynthesis and tetrapyrrole formation by the C5 pathway Acidithiobacillus ferrooxidans AMP + diphosphate + L-glutamyl-tRNAGlu
-
?
additional information GluRS plays a major role in regulating the cellular level of heme, aminoacylation of tRNAGlu correlates with the demand of heme, a transcriptional mechanism might control the level of GluRS1 in cells grown in Fe2+, under growth conditions in which cells do not require Glu-tRNA, as precursor for heme biosynthesis, up to 85% of GluRS1 is dispensable, but no major detrimental effect in the cell growth is observed. Thus, GluRS2 and the remaining 15% of the activity of GluRS1 are sufficient to provide the Glu-tRNA substrates for protein synthesis Acidithiobacillus ferrooxidans ?
-
?

Synonyms

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

Temperature Optimum [°C]

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
Acidithiobacillus ferrooxidans