EC Number   |
Inhibitors |
Structure |
|---|
   1.5.1.40 | 4-Chloromercuriphenyl sulfonate |
- |
   |
| 1.5.1.40 | aphloiol |
- |
|
| 1.5.1.40 | Baicalin |
- |
|
| 1.5.1.40 | beta-D-glucose pentaacetate |
- |
|
| 1.5.1.40 | frangulin A |
- |
|
| 1.5.1.40 | iodoacetamide |
- |
|
| 1.5.1.40 | mangiferin |
- |
|
| 1.5.1.40 | more |
the enzyme is not inhibited by iodoacetamide (20 mM), chloromercuribenzoate (20 mM) or N-ethylmaleimide (7 mM) when preincubated for 30 min in the presence of these reagents. The enzyme is not inactivated by dioxygen |
|
| 1.5.1.40 | more |
inhibitor prediction studies reveal that lovastatin and compactin (mevastatin) produced more affinity for model structure of NADP oxidoreducatse as compared to F420. It indicates that the lovastatin and compactin (mevastatin) compounds (negative regulator) may act as potential inhibitor of F420 dependent NADP oxidoreducatse protein |
|
| 1.5.1.40 | more |
inhibitor screening in a set of more than 8,000 naturally occurring small ligands and molecular docking, overview. Molecular flexibility, the number of H-bond acceptors and donors, the extent of hydrophobic interactions, and the exposure to the solvent are the major discriminants in determining the affinity of the ligands for enzyme FNO, that act in a competitive nature of the compounds of interest with NADP+ for the same site, causing a decrease in F420 reduction rates. Effects of pH and ionic strength on complex affinity |
|
