Application | Comment | Organism |
---|---|---|
biotechnology | supramolecular tandem assays exploit the dynamic binding of a fluorescent dye with a macrocyclic host in competition with the binding of the substrate and product. Two examples of enzymatic reactions were investigated: the hydrolysis of arginine to ornithine catalyzed by arginase and the oxidation of cadaverine to 5-aminopentanal by diamine oxidase, in which the substrates have a higher affinity to the macrocycle than the products (substrate-selective assays). The depletion of the substrate allows the fluorescent dye to enter the macrocycle in the course of the enzymatic reaction, which leads to the desired fluorescence response. For arginase, p-sulfonatocalix[4]arene is used as the macrocycle, and for diamine oxidase, cucurbit[7]uril (CB7) is used. An additional reporter pair, namely cucurbit[7]uril (CB7)/acridine orange (AO) is applied and the potential of tandem assays for inhibitor screening is demonstrated | Sus scrofa |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
KCN | - |
Sus scrofa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | enzyme isolated from | Sus scrofa | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cadaverine + H2O + O2 | - |
Sus scrofa | 5-aminopentanal + NH3 + H2O2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Amine oxidase | - |
Sus scrofa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Sus scrofa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Sus scrofa |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.21 | - |
- |
Sus scrofa | KCN |