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Inhibition of a Membrane‐Bound Enkephalin‐Degrading Aminopeptidase by Bestatin Analogs
Author(s) -
Shimamura Mariko,
Hazato Tadahiko,
Hachisu Mitsugu,
Katayama Takashi
Publication year - 1984
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1984.tb12816.x
Subject(s) - aminopeptidase , enkephalin , enzyme , biochemistry , chemistry , non competitive inhibition , substrate specificity , kinetics , substrate (aquarium) , membrane , stereochemistry , amino acid , biology , leucine , ecology , receptor , physics , quantum mechanics , opioid
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 AcOH, with a K i value of 0.21 × 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.