EC Number   |
Inhibitors |
Structure |
|---|
   3.4.13.20 | 3-(acetylamino)-L-alanyl-L-histidine |
2.3 mM, 50% inhibition of 3-nitrotyrosine formation |
   |
| 3.4.13.20 | 3-amino-L-alanyl-L-histidine |
3.3 mM, 50% inhibition of 3-nitrotyrosine formation |
|
| 3.4.13.20 | AgNO3 |
30°C, 10 min, 1 mM, 95% loss of activity |
|
| 3.4.13.20 | bestatin |
- |
|
| 3.4.13.20 | CdCl2 |
30°C, 10 min, 1 mM, 90% loss of activity |
|
| 3.4.13.20 | citrate |
citrate ions are shown to bind at only three well-defined sites involving both ion pairs and hydrogen bonds. Molecular dynamics simulations evidence that citrate binding has a remarkable conformational influence on the 3D structure of carnosinase, increasing the binding affinity of carnosine to the catalytic site |
|
| 3.4.13.20 | cysteine |
lowers dose-dependently recombinant CN1 efficiency |
|
| 3.4.13.20 | dithiothreitol |
30°C, 10 min, 1 mM, 63% loss of activity |
|
| 3.4.13.20 | EDTA |
- |
|
| 3.4.13.20 | HgCl2 |
30°C, 10 min, 1 mM, 99% loss of activity |
|
