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

BRENDA support

Literature summary extracted from

  • Harada, M.; Hiraoka, B.Y.; Fukasawa, K.M.; Fukasawa, K.
    Chemical modification of dipeptidyl peptidase iv: involvement of an essential tryptophan residue at the substrate binding site (1984), Arch. Biochem. Biophys., 234, 622-628.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.4.14.5 inactivation by photosensitization in presence of methylene blue Sus scrofa
3.4.14.5 modification of 4 His residues per subunit using diethyldicarbonate results in 30% inactivation Sus scrofa
3.4.14.5 N-bromosuccinimide almost completely inactivates with the modification of only one Trp residue per subunit, protective action of the substrate and inhibitors such as Ala-Pro-Ala and Pro-Pro Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.14.5 diethyldicarbonate modification of 4 His residues per subunit using diethyldicarbonate results in 30% inactivation Sus scrofa
3.4.14.5 N-bromosuccinimide almost completely inactivates with the modification of only one Trp residue per subunit, protective action of the substrate and inhibitors such as Ala-Pro-Ala and Pro-Pro Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.4.14.5 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.14.5 kidney
-
Sus scrofa
-