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6.1.1.17: glutamate-tRNA ligase

This is an abbreviated version!
For detailed information about glutamate-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.17

Reaction

ATP
+
L-glutamate
+
tRNAGlu
=
AMP
+
diphosphate
+
L-glutamyl-tRNAGlu

Synonyms

bifunctional aminoacyl-tRNA synthetase, bifunctional glutamate/proline-tRNA ligase, D-GluRS, discriminating GluRS, EC 2.7.2.13, Ec-GluRS, EPRS, ERS, Ers2, GltX, GluRS, GluRS1, GluRS2, GluRSAt, Glutamate--tRNA ligase, Glutamate-tRNA synthetase, Glutamic acid translase, Glutamic acid tRNA ligase, Glutaminyl-tRNA synthetase, Glutamyl tRNA synthetase, glutamyl-prolyl tRNA synthetase, glutamyl-prolyl-tRNA synthetase, glutamyl-Q tRNAASp synthetase, Glutamyl-transfer ribonucleate synthetase, Glutamyl-transfer ribonucleic acid synthetase, Glutamyl-transfer RNA synthetase, Glutamyl-tRNA synthetase, glutamyl-tRNAsynthetase, GtS, More, P85, surface-exposed glutamyl tRNA synthetase, TM1351, tRNA modifying enzyme, YadB

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.17 glutamate-tRNA ligase

Inhibitors

Inhibitors on EC 6.1.1.17 - glutamate-tRNA ligase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,2R)-1-(4-methylsulfonylphenyl)-2-(L-methionylsulfone-amido)-1,3-propanediol
-
-
(1R,2R)-1-(4-nitrophenyl)-2-(L-ethionyl-sulfoneamido)-1,3-propanediol
-
competitive inhibition with respect to Asp-tRNAAsn
(1R,2R)-1-phenyl-2-(L-methionyl-sulfone-amido)-1,3-propanediol
-
-
(1R,2S)-1-(4-nitrophenyl)-2-(L-methionyl-sulfoneamido)-1,3-propanediol
-
-
(1S,2R)-1-(4-nitrophenyl)-2-(L-methionyl-sulfoneamido)-1,3-propanediol
-
-
(1S,2S)-1-(4-nitrophenyl)-2-(L-methionyl-sulfone-amido)-1,3-propanediol
-
-
1,10-phenanthroline
-
ATP protects the enzyme against zinc removal
5'-O-(N'-(L-pyroglutamyl)-sulfamoyl)adenosine
-
weak
5'-O-(N-(L-glutamyl)-sulfamoyl)adenosine
5'-O-[N-(L-glutamyl)sulfamoyl]adenosine
i.e. glutamyl-sulfamoyl-adenosine or Glu-AMS, tRNAGlu increases the affinity of glutamyl-tRNA synthetase for its inhibitor glutamyl-sulfamoyl-adenosine, an analogue of the aminoacylation reaction intermediate glutamyl-AMP, thermodynamics of the enzyme-inhibitor interactions, overview. A significant entropic contribution for the interactions between Glu-AMS and GluRS in the absence of tRNA or in the presence of the cognate tRNAGlu or of the non-cognate tRNAPhe is indicated. The large negative enthalpy is the dominant contribution to DELTAGb in the absence of tRNA. The affinity of GluRS for Glu-AMS is not altered in the presence of the non-cognate tRNAPhe, but the dissociation constant Kd is decreased 50fold in the presence of tRNAGlu. Presence of an H-bond between Glu-AMS and the 3'-OH oxygen of the 3'-terminal ribose of tRNAGlu in the Glu-AMS/GluRS/tRNAGlu complex, molecular dynamics study
5'-O-[N-(Lglutamyl)sulfamoyl]adenosine
-
competitive inhibitor with respect to L-glutamate
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
chloramphenicol
-
-
diphosphate
erythro-4-Hydroxy-DL-glutamic acid
-
glutamate transfer to tRNA
erythro-gamma-methyl-L-glutamic acid
-
glutamate transfer to tRNA
gamma-Globulin
-
-
-
Glu-AMS
-
-
glutaminyl-beta-ketophosphonate-adenosine
-
i.e. Gln-KPA, competitive inhibition, non-cognate, binds at one site on the monomeric enzyme
glutamol-AMP
glutamyl adenylate
-
-
glutamyl cytidylate
-
weak inhibition
glutamyl dihydrocytidylate
-
very weak inhibition
glutamyl N6-benzoyladenylate
-
-
glutamyl uridylate
-
very weak inhibition
glutamyl-beta-ketophosphonate-adenosine
-
i.e. Glu-KPA, selective, competitive inhibition of GluRS, binds at one site on the monomeric enzyme
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
hemin
LiCl
-
100 mM, 22% inhibition of ATP-diphosphate exchange, 500 mM, 73% inhibition
N'-(3-chlorophenyl)-N-(5,5-dimethyl-3-[(E)-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]amino]-2-sulfanylidene-1,3-thiazolidin-4-yl)-N-hydroxyurea
competitive with glutamic acid but noncompetitive with ATP
N-(2,4-difluorophenyl)-N'-[4-[1-phenyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]phenyl]urea
noncompetitive with both ATP and glutamic acid
N6-Benzoyl-L-glutamyl AMP
-
specific for glutamyl-tRNA synthetase, does not inhibit glutaminyl-tRNA synthetase
NaCl
-
100 mM, 40% inhibition of ATP-diphosphate exchange, 500 mM, 91% inhibition
NH4Cl
-
100 mM, 31% inhibition of ATP-diphosphate exchange, 500 mM, 82% inhibition of ATP-diphosphate exchange
p-hydroxymercuribenzoate
-
-
threo-4-Hydroxy-L-glutamic acid
threo-4-Methyl-D-glutamic acid
additional information
-