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(1R,2R)-1-(4-methylsulfonylphenyl)-2-(L-methionylsulfone-amido)-1,3-propanediol
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(1R,2R)-1-(4-nitrophenyl)-2-(L-ethionyl-sulfoneamido)-1,3-propanediol
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competitive inhibition with respect to Asp-tRNAAsn
(1R,2R)-1-phenyl-2-(L-methionyl-sulfone-amido)-1,3-propanediol
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(1R,2S)-1-(4-nitrophenyl)-2-(L-methionyl-sulfoneamido)-1,3-propanediol
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(1S,2R)-1-(4-nitrophenyl)-2-(L-methionyl-sulfoneamido)-1,3-propanediol
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(1S,2S)-1-(4-nitrophenyl)-2-(L-methionyl-sulfone-amido)-1,3-propanediol
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1,10-phenanthroline
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ATP protects the enzyme against zinc removal
5'-O-(N'-(L-pyroglutamyl)-sulfamoyl)adenosine
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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
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competitive inhibitor with respect to L-glutamate
amino levulinic acid
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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
erythro-4-Hydroxy-DL-glutamic acid
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glutamate transfer to tRNA
erythro-gamma-methyl-L-glutamic acid
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glutamate transfer to tRNA
glutaminyl-beta-ketophosphonate-adenosine
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i.e. Gln-KPA, competitive inhibition, non-cognate, binds at one site on the monomeric enzyme
glutamyl cytidylate
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weak inhibition
glutamyl dihydrocytidylate
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very weak inhibition
glutamyl N6-benzoyladenylate
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glutamyl uridylate
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very weak inhibition
glutamyl-beta-ketophosphonate-adenosine
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i.e. Glu-KPA, selective, competitive inhibition of GluRS, binds at one site on the monomeric enzyme
H2O2
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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
LiCl
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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
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specific for glutamyl-tRNA synthetase, does not inhibit glutaminyl-tRNA synthetase
NaCl
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100 mM, 40% inhibition of ATP-diphosphate exchange, 500 mM, 91% inhibition
NH4Cl
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100 mM, 31% inhibition of ATP-diphosphate exchange, 500 mM, 82% inhibition of ATP-diphosphate exchange
p-hydroxymercuribenzoate
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threo-4-Hydroxy-L-glutamic acid
threo-4-Methyl-D-glutamic acid
5'-O-(N-(L-glutamyl)-sulfamoyl)adenosine
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potent competitive with respect to glutamic acid
5'-O-(N-(L-glutamyl)-sulfamoyl)adenosine
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potent competitive with respect to glutamic acid
diphosphate
competitive to ATP and L-glutamate, uncompetitive to tRNAGlu
glutamol-AMP
noncompetitive to ATP and L-glutamate
glutamol-AMP
competitive inhibition
heme
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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
hemin
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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
hemin
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GluRS1 activity is reversibly inactivated upon oxidation by hemin. tRNAGlu is able to protect GluRS1 against oxidative inactivation by hemin plus hydrogen peroxide
KCl
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aminoacylation
KCl
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100 mM, 15% inhibition of ATP-diphosphate exchange, 500 mM, 62% inhibition
threo-4-Hydroxy-L-glutamic acid
Caesalpinia bondue
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glutamate transfer to tRNA
threo-4-Hydroxy-L-glutamic acid
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glutamate transfer to tRNA
threo-4-Methyl-D-glutamic acid
Caesalpinia bondue
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glutamate transfer to tRNA
threo-4-Methyl-D-glutamic acid
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glutamate transfer to tRNA
additional information
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ERS aminoacylation of tRNAGlu is inhibited by the tRNA fragments, RNA-protein interactions, ERS binding of minihelixGlu and fragments ASLGlu and ASLGlu-s2U34, overview
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additional information
screening of 890 synthetic compounds for inhibitory activity against enzyme GluRS, fourteen compounds with inhibitory activity are identified, overview. Minimum inhibitory concentrations (MICs) are determined for each of the compounds against a panel of pathogenic bacteria
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additional information
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screening of 890 synthetic compounds for inhibitory activity against enzyme GluRS, fourteen compounds with inhibitory activity are identified, overview. Minimum inhibitory concentrations (MICs) are determined for each of the compounds against a panel of pathogenic bacteria
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additional information
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rGtS and anti-rGtS antiserum significantly inhibits the adhesion of 3 pairs of encapsulated and unencapsulated strains of Streptococcus pneumoniae to human epithelial A549 cells
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