Are diprotin A (Ile-Pro-Ile) and diprotin B (Val-Pro-Leu) inhibitors or substrates of dipeptidyl peptidase IV?

doi:10.1016/0167-4838(91)90284-7

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Volume 1076, Issue 2, 29 January 1991, Pages 314-316

Biochimica et Biophy...

https://doi.org/10.1016/0167-4838(91)90284-7 Get rights and content

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 compoundas 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.

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Are diprotin A (Ile-Pro-Ile) and diprotin B (Val-Pro-Leu) inhibitors or substrates of dipeptidyl peptidase IV?

Abstract

Biochim. Biophys. Acta

Biochim. Biophys. Acta