Lebouille J L, Visser W H, Hendriks R W, Van Nispen J W, Greven H M, Burbach J P
Biochem Biophys Res Commun. 1985 Dec 31;133(3):897-903. doi: 10.1016/0006-291x(85)91220-3.
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.
γ-内啡肽生成内肽酶（γEGE）活性是一种将β-内啡肽转化为γ-内啡肽和β-内啡肽-（18-31）的酶活性。测试了神经肽及其类似物或片段对γEGE活性的抑制效力。强啡肽-（1-13）（IC50：0.14微摩尔）、人β-内啡肽-（1-31）（IC50：15.5微摩尔）、猪促肾上腺皮质激素-（1-39）（IC50：6.3微摩尔）和P物质（IC50：26微摩尔）对γEGE活性具有抑制活性。β-内啡肽-（18-31）（IC50：0.35微摩尔）而非γ-内啡肽能有效抑制γEGE活性。聚（Lys）40-60的IC50为0.8微摩尔。得出以下结论：1）γEGE活性受到其产物β-内啡肽-（18-31）的强烈抑制；2）该酶受到在肽链NH2末端具有芳香族氨基酸和/或在COOH末端具有碱性氨基酸的肽的强烈抑制。
