Cleavage of p-nitroanilides of N-acylated tri- and tetrapeptides by alanine endopeptidase from the brush border membranes of rat enterocytes.
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.
D000818:Animals; D002863:Chromogenic Compounds / Q000378:metabolism; D007422:Intestines / Q000648:ultrastructure*; D008871:Microvilli / Q000201:enzymology; D009842:Oligopeptides / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity
D002863:Chromogenic Compounds; D009842:Oligopeptides; C015516:succinyl-trialanine-4-nitroanilide