EC Number |
Ki Value [mM] |
Ki Value maximum [mM] |
Inhibitor |
Reference |
---|
4.1.1.28 | -999 |
- |
more |
Samples containing varying amounts of the purified molecule are incubated in the presence of 0.34 U Ddc from mouse kidney homogenate at room temperature for 15 min. This results in an inhibitor quantity-dependent increase of Ddc activity inhibition. The inhibitory activity reaches saturation, when 1.8 microg of purified inhibitor are added to the reaction. Samples containing 0.9 microg of the purified inhibitor are incubated in the presence of 0.34 U Ddc from mouse kidney homogenate for varying time periods at room temperature, prior to estimation of their inhibitory activity. The purified molecule causes a time-dependent inhibition of Ddc, while there is no inhibitory activity at 0 min. The inhibitory activity is seen to reach a maximum effect at 30 min, before declining. |
694362 |
4.1.1.28 | 0.000036 |
- |
annexin 5 |
inhibitor purified from mouse kidney homogenate ddc, classical non-competitive inhibitor |
694362 |
4.1.1.28 | 0.0005 |
- |
Amb2470350 |
pH and temperature not specified in the publication |
746908 |
4.1.1.28 | 0.0018 |
- |
4-[(E)-[(3-phenyl-5-sulfanyl-4H-1,2,4-triazol-4-yl)imino]methyl]benzene-1,2-diol |
pH 7.4, 25°C |
728566 |
4.1.1.28 | 0.0023 |
- |
4-[(E)-[[3-(4-chlorophenyl)-5-sulfanyl-4H-1,2,4-triazol-4-yl]imino]methyl]benzene-1,2-diol |
pH 7.4, 25°C |
728566 |
4.1.1.28 | 0.0044 |
- |
2-[[(2-oxo-2,3-dihydro-1H-benzimidazol-5-yl)sulfonyl]amino]-N-phenylbenzamide |
pH 7.4, 25°C |
728566 |
4.1.1.28 | 0.0151 |
- |
4-[(E)-[(3-phenyl-5-sulfanyl-4H-1,2,4-triazol-4-yl)imino]methyl]benzene-1,2,3-triol |
pH 7.4, 25°C |
728566 |
4.1.1.28 | 0.31 |
- |
tryptamine |
- |
653443 |
4.1.1.28 | 5.7 |
- |
5-hydroxy-L-tryptophan |
wild-type enzyme, the data of initial velocity for decarboxylation of 5-hydroxy-L-tryptophan versus substrate concentration exhibit a substrate-inhibition pattern that requires a modified version of the Michaelis-Menten equation. |
690973 |
4.1.1.28 | 10 |
- |
L-Dopa |
wild-type enzyme, the data of initial velocity for decarboxylation of L-dopa versus substrate concentration curiously exhibit a substrate-inhibition pattern that requires a modified version of the Michaelis-Menten equation. |
690973 |