Effect of various enkephalin analogs and dipeptides on the enzymatic activity of enkephalinase B isolated from calf-brain striatum.
The inhibitory potency of several enkephalin analogs and dipeptides on the calf-brain enkephalinase B activity was established with the aim to characterize its active site. Highest potency was measured for dipeptides with a large side chain on both amino acids. The nature of the distal amino acid is of minor importance, provided it is not a glycine. Free carboxylic function is required for good interaction, whereas the stereochemical configuration of the dipeptide is less so. Enkephalinase B has only little affinity for D-Ala2-Leu-enkephalin. The data are to be used for the design of new enkephalinase B inhibitors.
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002417:Cattle; D003342:Corpus Striatum / Q000201:enzymology*; D004151:Dipeptides / Q000494:pharmacology*; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000037:antagonists & inhibitors*; D010450:Endopeptidases / Q000378:metabolism*; D004745:Enkephalins / Q000494:pharmacology*; D007700:Kinetics; D010446:Peptide Fragments / Q000494:pharmacology; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D004151:Dipeptides; D004745:Enkephalins; D010446:Peptide Fragments; D010450:Endopeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C100152:dipeptidyl peptidase III