Inhibition of a membrane-bound enkephalin-degrading aminopeptidase by bestatin analogs.
A variety of bestatin analogs were examined as potent inhibitors of a membrane-bound enkephalin-degrading aminopeptidase that was purified from monkey brain. Bestatinyl amino acid derivatives showed strong inhibition of this enzyme. The most effective was bestatin-L-Arg X AcOH, with a Ki value of 0.21 X 10(-8) M with Leu-enkephalin as substrate. It exhibited competitive kinetics and was about 100-fold more potent than bestatin. This compound seems to be useful for pharmacological and other studies.
D000626:Aminopeptidases / Q000037:antagonists & inhibitors*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D000882:Haplorhini; D007700:Kinetics; D007930:Leucine / Q000031:analogs & derivatives* / Q000494:pharmacology; D013329:Structure-Activity Relationship
D000626:Aminopeptidases; C025579:enkephalin degrading enzyme; D007930:Leucine; C012211:ubenimex