EC Number   |
Inhibitors |
Structure |
|---|
    1.14.15.6 | (20R,S)-20-amino-5-pregnen-3beta-ol |
20-amine derivative, amine is attached closer to the D-ring than in the 22-amine, very weak inhibitor, 0.1 mM causes less than 20% inhibition |
   |
| 1.14.15.6 | (20S)-22-thiacholesterol |
competitive inhibitor, is converted enzymatically to a more potent inhibitor, the (22S) and (22R) sulfoxides, inhibition by approximately 75% at 0.001 mM, no inactivation in absence of NADPH and O2 |
|
| 1.14.15.6 | (20S,22R)-22-thiacholesterol S-oxide |
competitive versus cholesterol, binds 10times more tightly than (22S) diastereomer, 25% and 44% inhibition at 0.00005 mM and 0.0001 mM, respectively, complete inhibition at 0.001 mM, no substrate for P-450 |
|
| 1.14.15.6 | (20S,22S)-22-thiacholesterol S-oxide |
competitive versus cholesterol, no substrate for P-450 |
|
| 1.14.15.6 | (22R)-22-Aminocholesterol |
completely inhibited by 0.001 mM, affinity toward the P-450scc almost 3fold greater than that for the (22S) form, competitive versus cholesterol, no substrate for P-450 |
|
| 1.14.15.6 | (22S)-22-Aminocholesterol |
not inhibited below 0.001 mM, competitive versus cholesterol, no substrate for P-450 |
|
| 1.14.15.6 | 17,20-dihydroxyvitamin D2 |
competitive inhibitor |
|
| 1.14.15.6 | 17beta-amino-5-androsten-3beta-ol |
17-amine derivative, amine is attached closer to the D-ring than in the 22-amine, very weak inhibitor, 0.1 mM causes less than 20% inhibition |
|
| 1.14.15.6 | 22-Amino-23,24-bisnor-5-cholen-3beta-ol |
22-amine derivative, same steroid ring structure as cholesterol, competitive inhibitor with respect to cholesterol, 50% reversible inhibition at 0.0001 mM, reversible cooperative binding |
|
| 1.14.15.6 | 22-Amino-23,24-bisnor-5-cholen-3beta-ol |
22-amine derivative, same steroid ring structure as cholesterol, competitive inhibitor with respect to cholesterol, 50% reversible inhibition at 0.0001 mM, reversible cooperative binding; dual interaction: binding of steroid ring to cholesterol site and bonding of the amine to the heme iron. need not be metabolically activated in order to inhibit the enzyme, not metobolized to pregnenolone. 60% competitive inhibition at 0.00015 mM |
|
