BRENDA - Enzyme Database show

Regulation of a glutamyl-tRNA synthetase by the heme status

Levican, G.; Katz, A.; de Armas, M.; Nunez, H.; Orellana, O.; Proc. Natl. Acad. Sci. USA 104, 3135-3140 (2007)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
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
Commentary
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
Commentary
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
Commentary
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
Commentary
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
Commentary
Organism
Structure
6.1.1.17
Mg2+
-
Acidithiobacillus ferrooxidans
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
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
Commentary
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
Commentary
Organism
1.2.1.70
-
Acidithiobacillus ferrooxidans
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
676889
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
676889
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
676889
Acidithiobacillus ferrooxidans
?
-
-
-
-
Temperature Optimum [C]
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
6.1.1.17
37
-
assay at
Acidithiobacillus ferrooxidans
Cofactor
EC Number
Cofactor
Commentary
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
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
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 (protein specific)
EC Number
Application
Commentary
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) (protein specific)
EC Number
Commentary
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
Cofactor (protein specific)
EC Number
Cofactor
Commentary
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
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
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] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
6.1.1.17
additional information
-
additional information
steady-state kinetics of isozymes GluRS1 and GluRS2
Acidithiobacillus ferrooxidans
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.17
Mg2+
-
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
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
?
-
-
-
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
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) (protein specific)
EC Number
Commentary
Organism
1.2.1.70
-
Acidithiobacillus ferrooxidans
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
676889
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
676889
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
676889
Acidithiobacillus ferrooxidans
?
-
-
-
-
Temperature Optimum [C] (protein specific)
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
6.1.1.17
37
-
assay at
Acidithiobacillus ferrooxidans