EC Number   |
Inhibitors |
Structure |
|---|
   5.3.4.1 | 1,1-bis(4-hydroxyphenyl)ethane |
i.e.bisphenol E, 15% inhibition at 0.0125 mM |
   |
| 5.3.4.1 | 1,3-diphenylpropane |
8% inhibition at 0.0125 mM |
|
| 5.3.4.1 | 12-O-Tetradecanoylphorbol 13-acetate |
binds to and moderately inhibits PDI |
|
| 5.3.4.1 | 16F16 |
irreversible inhibition |
|
| 5.3.4.1 | 2',3,3',4',5'-pentachlorobiphenyl |
strong inhibition of PDI 3,3',5-triiodo-L-thyronine-binding activity |
|
| 5.3.4.1 | 2',3,3',5,5',6'-hexachlorobiphenyl |
strong inhibition of PDI 3,3',5-triiodo-L-thyronine-binding activity |
|
| 5.3.4.1 | 2,2-bis(4-hydroxyphenyl)propane |
i.e. bisphenol A, 30% inhibition at 0.0125 mM |
|
| 5.3.4.1 | 2,4-dinitrochlorobenzene |
- |
|
| 5.3.4.1 | 2-(2-carboxy-4-nitro-phenyl) disulfonyl-5-nitrobenzoic acid |
i.e. NSC517871. Molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored |
|
| 5.3.4.1 | 2-nitro-5-sulfo-sulfonyl-benzoic acid |
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored |
|
