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  • Title: [Inhibition of aminopeptidase activity of rat small intestine by the tripeptide H-Thr-(O-tert. butyl)-Phe-Pro-OH].
    Author: Friedrich M, Uhlig J, Noack R.
    Journal: Acta Biol Med Ger; 1978; 37(10):1513-22. PubMed ID: 752204.
    Abstract:
    The hydrolysis of L-leucine-beta-naphthylamide and L-leucinamide by leucinaminopeptidase (E.C. 3.4.11.1) from bovine eye lens is inhibited by H-Thr (O-tert. butyl)-Phe-Pro-OH. The inhibitor constants are Ki = 1.5 . 10(-5) M and 0.8 . 10(-5) M, respectively. Both brush border peptidases, leucinarylamidase (E.C. 3.4.11.2) AND TRIPEPTIDASE (E.C. 3.4.11.4), are inhibited to a smaller extent (Ki = 0.8 . 10(-3) M). Mn++-ions activate the cytosolic leucinaminopeptidase but not the hydrolysis of leucinamide by the brush border arylamidase. The inhibition of the cytosolic leucinamidase by the peptide (Ki = 3.5 . 10(-4)) is twice as that of the brush border arylamidase.
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