Literature summary for 3.4.14.5 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.

Search for more literature for 3.4.14.5

General Stability

General Stability	Organism
inactivation by photosensitization in presence of methylene blue	Sus scrofa
modification of 4 His residues per subunit using diethyldicarbonate results in 30% inactivation	Sus scrofa
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

Inhibitors	Comment	Organism	Structure
diethyldicarbonate	modification of 4 His residues per subunit using diethyldicarbonate results in 30% inactivation	Sus scrofa
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

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
kidney	-	Sus scrofa	-

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Release 2023.1 (January 2023)