Inhibition of gamma-endorphin generating endopeptidase activity of rat brain by peptides: structure activity relationship.
gamma-Endorphin generating endopeptidase (gamma EGE) activity is an enzyme activity which converts beta-endorphin into gamma-endorphin and beta-endorphin-(18-31). The inhibitory potency on gamma EGE activity of neuropeptides and analogues or fragments of neuropeptides was tested. Dynorphin-(1-13) (IC50: 0.14 microM), human beta-endorphin-(1-31) (IC50: 15.5 microM), porcine ACTH-(1-39) (IC50: 6.3 microM), and substance P (IC50: 26 microM) had an inhibitory activity on gamma EGE activity. beta-Endorphin-(18-31) (IC50: 0.35 microM) but not gamma-endorphin potently inhibited gamma EGE activity. The IC50 of poly (Lys)40-60 was 0.8 microM. It is concluded that 1) gamma EGE activity is strongly inhibited by its product beta-endorphin-(18-31), 2) the enzyme is strongly inhibited by peptides with an aromatic amino acid at the NH2-terminal and/or basic amino acids in the COOH-terminal of the peptide chain.
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology*; D055598:Chemical Phenomena; D002621:Chemistry; D010450:Endopeptidases / Q000378:metabolism; D007700:Kinetics; D009419:Nerve Tissue Proteins / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology*; D011480:Protease Inhibitors; D051381:Rats; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D011480:Protease Inhibitors; D010450:Endopeptidases; C043537:gamma-endorphin generating enzyme