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Literature summary 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

EC Number Activating Compound Comment Organism Structure
1.2.1.70 heme under high heme requirement for respiration levels of GluTR increase Acidithiobacillus ferrooxidans
6.1.1.17 additional information under high heme requirement for respiration increased levels of GluRS occur Acidithiobacillus ferrooxidans

Application

EC Number Application Comment Organism
1.2.1.70 additional information the function of GluTR is regulated by mechanisms that involve the steady-state level of the protein or the activity of the enzyme in response to the cellular heme status Acidithiobacillus ferrooxidans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.70 His(6)-GluTR overexpressed in Escherichia coli BL21 (DE3) Acidithiobacillus ferrooxidans
6.1.1.17 overexpression of GST-tagged isozyme GluRS1 in Escherichia coli strain Bl21(DE3), co-expression with Glu-tRNA reductase Acidithiobacillus ferrooxidans

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.70 heme when intracellular heme is in excess, the cells respond by a dramatic decrease of the level of GluTR Acidithiobacillus ferrooxidans
6.1.1.17 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
6.1.1.17 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
6.1.1.17 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]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.17 Mg2+
-
 Acidithiobacillus ferrooxidans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.17 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
-
 ?
6.1.1.17 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

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.1.1.17 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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.70
-
 Acidithiobacillus ferrooxidans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Acidithiobacillus ferrooxidans AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 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
-
 ?
6.1.1.17 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

EC Number Synonyms Comment Organism
1.2.1.70 GluTR
-
 Acidithiobacillus ferrooxidans
6.1.1.17 GluRS
-
 Acidithiobacillus ferrooxidans
6.1.1.17 Glutamyl-tRNA synthetase
-
 Acidithiobacillus ferrooxidans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.17 37
-
 assay at Acidithiobacillus ferrooxidans

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.70 heme the levels of GluTR are regulated by the heme status Acidithiobacillus ferrooxidans
6.1.1.17 ATP
-
 Acidithiobacillus ferrooxidans