Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.4 extracted from

  • Wang, Y.Q.; Zhang, H.M.
    Effects of bisphenol S on the structures and activities of trypsin and pepsin (2014), J. Agric. Food Chem., 62, 11303-11311.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Sus scrofa
-
pancreas
-
Sus scrofa
-