(Journal Article): Are diprotin A (Ile-Pro-He) and diprotin B (Val-Pro-Leu) inhibitors or substrates for dipeptidyl peptidase IV?
 
Rahfeld J, Schierhorn M, Hartrodt B, Neubert K, Heins J (Martin-Luther-University, Biotechnikum Halle, F.R.G.)
 
IN: Biochim Biophys Acta 1991; 1076:314-316

ABSTRACT: Dipeptidyl peptidase IV preferably hydrolyzes peptides and proteins with a penultimate proline residue. Umezawa and co-workers (Umezawa et al. (1984) J. Antibiotics 37, 422-425) reported that diprotin A (Ile-Pro-Ile) and diprotin B (Val-Pro-Leu) are inhibitors for dipeptidyl peptidase IV. We could show that both compounds as well as other tripeptides with a penultimate proline residue are substrates for dipeptidyl peptidase IV. An apparent competitive inhibition by those compounds is a kinetic artifact due to the substrate-like structure of such tripeptides.

TYPE OF PUBLICATION: Original article

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