EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.4 | bisphenol A | the secondary and tertiary structures of trypsin are altered by bisphenol S binding, which results in the loosening of the skeleton of the enzyme. Bisphenol S induces microenvironmental changes around tyrosine and tryptophan residues of trypsin. The activity of trypsin does not change remarkably with the increasing concentration of bisphenol S. The binding of bisphenol S to trypsin is a spontaneous process and hydrogen bonding and hydrophobic interactions play a vital role in stabilizing the bisphenol S-trypsin complex. The binding constants of bisphenol S with trypsin are 74200 (25°C) and 59100 L/mol (37°C) | Sus scrofa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.4 | Sus scrofa | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.4.21.4 | commercial preparation | - |
Sus scrofa | - |
3.4.21.4 | pancreas | - |
Sus scrofa | - |