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Literature summary for 1.2.1.70 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
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Activating Compound

Activating Compound Comment Organism Structure
heme under high heme requirement for respiration levels of GluTR increase Acidithiobacillus ferrooxidans

Application

Application Comment Organism
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)

Cloned (Comment) Organism
His(6)-GluTR overexpressed in Escherichia coli BL21 (DE3) Acidithiobacillus ferrooxidans

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Acidithiobacillus ferrooxidans
-
 strain ATCC 23270
-

Purification (Commentary)

Purification (Comment) Organism
-
 Acidithiobacillus ferrooxidans

Synonyms

Synonyms Comment Organism
GluTR
-
 Acidithiobacillus ferrooxidans

Cofactor

Cofactor Comment Organism Structure
heme the levels of GluTR are regulated by the heme status Acidithiobacillus ferrooxidans