Christner C, Zerlin M, Gräfe U, Heinze S, Küllertz G, Fischer G
Max-Planck-Arbeitsgruppe Enzymologie der Peptidbindung, Halle/Saale, Germany.
J Antibiot (Tokyo). 1997 May;50(5):384-9. doi: 10.7164/antibiotics.50.384.
The new proline-containing lipohexapeptide lipohexin (I) isolated from three fungal strains, Moeszia lindtneri (HKI-0054) and Paecilomyces sp. (HKI-0055 and HKI-0096) is a competitive inhibitor of prolyl endopeptidase (PEP) from human placenta with IC50 of 3.5 microM. Specificity of lipohexin (I) is indicated by the much weaker inhibitory activity against bacterial prolyl endopeptidase from Flavobacterium meningosepticum (IC50 25 microM). No effect of lipohexin (I) was found on the activity of mechanistically related proteases such as proline specific proteases and other serine proteases.
从三种真菌菌株,即林氏莫氏霉菌(HKI-0054)和拟青霉属(HKI-0055和HKI-0096)中分离出的新型含脯氨酸脂环六肽脂环素(I),是一种来自人胎盘的脯氨酰内肽酶(PEP)的竞争性抑制剂,IC50为3.5微摩尔。脂环素(I)对来自脑膜炎败血黄杆菌的细菌脯氨酰内肽酶的抑制活性弱得多(IC50为25微摩尔),这表明了其特异性。未发现脂环素(I)对机械相关蛋白酶如脯氨酸特异性蛋白酶和其他丝氨酸蛋白酶的活性有影响。