title: Cleavage of p-nitroanilides of N-acylated tri- and tetrapeptides by alanine endopeptidase from the brush border membranes of rat enterocytes.
abstract: The activity of the alanine endopeptidase from the intestinal brush border was studied using chromogenic substrates of the general formula Sc-Ala2-X-pNA. Sc-Y-Z-Ala-pNA and W-Ala3-pNA respectively. Substrates with C-terminal Leu or Nle are hydrolyzed more readily than Ala-analogues. At least one Ala-residue in one of the positions adjacent to the C-terminus is necessary for the enzyme activity. An Na-substituent has no effect on the activity.
mesh_terms: D000818:Animals; D002863:Chromogenic Compounds / Q000378:metabolism; D007422:Intestines / Q000648:ultrastructure*; D008871:Microvilli / Q000201:enzymology; D009842:Oligopeptides / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity
chemical_list: D002863:Chromogenic Compounds; D009842:Oligopeptides; C015516:succinyl-trialanine-4-nitroanilide