EC Number   |
Inhibitors |
Structure |
|---|
    6.1.1.17 | (1R,2R)-1-(4-methylsulfonylphenyl)-2-(L-methionylsulfone-amido)-1,3-propanediol |
- |
   |
| 6.1.1.17 | (1R,2R)-1-(4-nitrophenyl)-2-(L-ethionyl-sulfoneamido)-1,3-propanediol |
competitive inhibition with respect to Asp-tRNAAsn |
|
| 6.1.1.17 | (1R,2R)-1-phenyl-2-(L-methionyl-sulfone-amido)-1,3-propanediol |
- |
|
| 6.1.1.17 | (1R,2S)-1-(4-nitrophenyl)-2-(L-methionyl-sulfoneamido)-1,3-propanediol |
- |
|
| 6.1.1.17 | (1S,2R)-1-(4-nitrophenyl)-2-(L-methionyl-sulfoneamido)-1,3-propanediol |
- |
|
| 6.1.1.17 | (1S,2S)-1-(4-nitrophenyl)-2-(L-methionyl-sulfone-amido)-1,3-propanediol |
- |
|
| 6.1.1.17 | 1,10-phenanthroline |
ATP protects the enzyme against zinc removal |
|
| 6.1.1.17 | 5'-O-(N'-(L-pyroglutamyl)-sulfamoyl)adenosine |
weak |
|
| 6.1.1.17 | 5'-O-(N-(L-glutamyl)-sulfamoyl)adenosine |
potent competitive with respect to glutamic acid |
|
| 6.1.1.17 | 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 |
|
