EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.25 | diisopropyl fluorophosphate | synthesis of denatured diisopropyl phosphorylcucumisin derivatives, which are hydrolyzed by chymotrypsin, to get peptides for amino acid sequence analysis around the reactive serine of the active site | Cucumis melo |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.25 | Protein + H2O | Cucumis melo | - |
? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.25 | Cucumis melo | - |
L. var Prince | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.4.21.25 | fruit | - |
Cucumis melo | - |
EC Number | Storage Stability | Organism |
---|---|---|
3.4.21.25 | lyophilization causes a loss of activity of more than 10% | Cucumis melo |
3.4.21.25 | very stable in a frozen solution, no loss of activity after one year | Cucumis melo |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.25 | casein + H2O | - |
Cucumis melo | ? | - |
? | |
3.4.21.25 | Protein + H2O | - |
Cucumis melo | ? | - |
? | |
3.4.21.25 | protein + H2O | - |
Cucumis melo | hydrolyzed protein | - |
? |