EC Number | Application | Comment | Organism |
---|---|---|---|
1.4.3.22 | 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 |
3.5.3.1 | analysis | assay method based on a combination of moderately selective host-guest binding with the specificity of enzymatic transformations which allows the real-time monitoring of enzymatic reactions in a homogeneous solution. The resulting 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. 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, which displays binding constants of 6400 per M with arginine, 550 per M with ornithine, and 60 000 per M with the selected fluorescent dye 1-aminomethyl-2,3-diazabicyclo[2.2.2]oct-2-ene, the dye shows a weaker fluorescence in its complexed state, which leads to a switch-off fluorescence response in the course of the enzymatic reaction. Assays can be successfully used to probe the inhibition of enzymes | Bos taurus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.22 | KCN | - |
Sus scrofa | |
3.5.3.1 | 2-(S)-amino-6-boronohexanoic acid | - |
Bos taurus | |
3.5.3.1 | S-(2-boronoethyl)-L-cysteine | - |
Bos taurus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.3.22 | Sus scrofa | - |
- |
- |
3.5.3.1 | Bos taurus | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.4.3.22 | kidney | enzyme isolated from | Sus scrofa | - |
3.5.3.1 | commercial preparation | - |
Bos taurus | - |
3.5.3.1 | liver | - |
Bos taurus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.22 | cadaverine + H2O + O2 | - |
Sus scrofa | 5-aminopentanal + NH3 + H2O2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.3.22 | Amine oxidase | - |
Sus scrofa |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.4.3.22 | 37 | - |
assay at | Sus scrofa |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.4.3.22 | 7.4 | - |
assay at | Sus scrofa |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.3.1 | 0.00015 | - |
2-(S)-amino-6-boronohexanoic acid | pH 9.5, 25°C, supramolecular tandem assay method | Bos taurus | |
3.5.3.1 | 0.0036 | - |
S-(2-boronoethyl)-L-cysteine | pH 9.5, 25°C, supramolecular tandem assay method | Bos taurus |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
1.4.3.22 | 0.21 | - |
- |
Sus scrofa | KCN | |
3.5.3.1 | 0.00022 | - |
pH 9.5, 25°C, supramolecular tandem assay method | Bos taurus | 2-(S)-amino-6-boronohexanoic acid | |
3.5.3.1 | 0.0037 | - |
pH 9.5, 25°C, supramolecular tandem assay method | Bos taurus | S-(2-boronoethyl)-L-cysteine |