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Are Diprotin A (Ile-Pro-Ile) and Diprotin B (Val-Pro-Leu) Inhibitors or Substrates of Dipeptidyl Peptidase IV?

J Rahfeld, M Schierhorn, B Hartrodt, K Neubert, J Heins

Biochim Biophys Acta. 1991 Jan 29;1076(2):314-6.

PMID: 1671823

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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP90614485 Ile-Pro-Ile Ile-Pro-Ile 90614-48-5 Price
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