EC Number   |
Inhibitors |
Structure |
|---|
    1.4.3.1 | (5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone |
i.e. thiolactomycin, active site-directed DDO inhibitor, competitive inhibition, competes with both the substrate and the coenzyme FAD; i.e. thiolactomycin, competitive inhibition, competes with both the substrate and the coenzyme FAD |
   |
| 1.4.3.1 | (5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone |
i.e. thiolactomycin, active site-directed DDO inhibitor involving binding via Arg237, mixed type of inhibition, competes with both the substrate and the coenzyme FAD, structural models of mouse DDO/TLM complexes; i.e. thiolactomycin, competitive inhibition, competes with both the substrate and the coenzyme FAD |
|
| 1.4.3.1 | 1-hydroxy-1H-indole-2-carboxylic acid |
- |
|
| 1.4.3.1 | 2-amino-5-chlorobenzoic acid |
- |
|
| 1.4.3.1 | 2-amino-5-methylthiophene-3-carboxylic acid |
- |
|
| 1.4.3.1 | 2-aminopyridine-3-carboxylic acid |
- |
|
| 1.4.3.1 | 2-aminopyridine-4-carboxylic acid |
- |
|
| 1.4.3.1 | 2-hydroxy-6-methylpyridine-3-carboxylic acid |
- |
|
| 1.4.3.1 | 2-oxoglutaric acid |
at 6.67 mM 64% inhibition |
|
| 1.4.3.1 | 3-aminobenzoic acid |
- |
|
