EC Number   |
Inhibitors |
Structure |
|---|
   3.5.1.78 | gamma-Glu-Ala-Gly-CHO |
most probably captures Cys59 and accumulates as the tetrahedral adduct in the amidase active site. Binding of phosphinophosphate in the Gsp synthetase active site potentiates the inhibition affinity for the aldehyde at the Gsp amidase active site by two orders of magnitude |
   |
| 3.5.1.78 | H2O2 |
50% inhibition with 0.25 mM. Inactivation is above 95% with 0.5 mM H2O2 for 5 min. Cysteine thiol of the GspSA amidase active-site nucleophile Cys59 is transiently inactivated by H2O2 oxidation to sulfenic acid which leads to an accumulation of glutathionylspermidine and an increased level of glutathionylspermidine S-thiolated proteins after oxidative stress. The hypersensitivities of GspSA and GspSA/glutaredoxin null mutants to H2O2 support the idea that GspSA and glutaredoxin act synergistically to regulate the redox environment of Escherichia coli |
|
| 3.5.1.78 | H2O2 |
- |
|
| 3.5.1.78 | iodoacetamide |
- |
|
| 3.5.1.78 | L-gamma-glutamyl-5-azido-N-(3-[[(4-methylphenyl)sulfonyl]oxy]-2-oxopropyl)-L-norleucinamide |
- |
|
| 3.5.1.78 | L-gamma-glutamyl-5-azido-N-[3-(benzoyloxy)-2-oxopropyl]-L-norleucinamide |
- |
|
| 3.5.1.78 | L-gamma-glutamyl-N-[3-(benzoyloxy)-2-oxopropyl]-6-[4-([[5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanoyl]amino]methyl)-1H-1,2,3-triazol-1-yl]-L-norleucinamide |
- |
|
| 3.5.1.78 | Polyamine-containing phosphopeptides |
potent and selective inhibitors, which selectively inhibit the synthetase domain over the amidase domain |
|
