Enzymatic Cleavage of the ϵ-Peptide Bond in α- and ϵ-Substituted Glycyl- and Phenylaianyl-Lysine Peptides

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Abstract
The title peptides were synthesized, following classic or non-classic routes. Some bacterial and mammalian enzymes, endo- and exo-peptide hydrolases of the enzyme nomenclature type EC 3.4., were tested for their ability to split the .epsilon.-peptide bond in the these substrates. Kinetic constants (Km, kcat) were evaluated with leucine aminopeptidase from hog kidney and eye lens and with aminopeptidase I from yeast. Aminopeptidase M (hog pancreas) and hog intestinal aminopeptidase were additionally examined for the Ki values with the above substrates in comparison to the classic protease substrate leucine p-nitroanilide. The intestinal mucosa hydrolases are especially efficient in cleaving .epsilon.-peptide bonds.