Biochemical characterization of endothelin converting enzyme

1.在猪肺膜组分中检测到两种对磷酰胺敏感的中性金属蛋白水解酶(M1和M2)，它们具有内皮素转化活性。M1仅专门将大ET-1转换为ET-1，而不是将大ET-2和大ET-3分别转换为ET-2和ET-3。结合其他生化分析，认为M1是一种新的生理酶，M2可能是已知的中性内肽酶2。(1)对内皮素-2(ET-2)生物合成途径的分析表明，ET-2是通过BIG ET-2(1-38)作为中间体产生的。ET-2转换酶(ECE2)的生化特性表明，ECE2是一种对磷酰胺敏感的金属蛋白水解酶，与内皮细胞中的内皮素-1转换酶(ECE1)非常相似。

1. Two phosphoramidon sensitive-neutral metalproteases (M1 and M2) with endothelin converting activity were detected in membranous fractions of porcine lung. M1 specifically converts only big ET-1 to ET-1 not big ET-2 and big ET-3 to ET-2 and ET-3, respectively. Taking together with other biochemical analyses, it is suggested that M1 is a new physiological enzyme and M2 may be a known neutral endopeptidase2. (i) Analysis of endothelin-2 (ET-2) biosynthetic pathway showed that ET-2 is produced via big ET-2(1-38) as an intermediate form. The biochemical characterization of ET-2 converting enzyme (ECE-2) indicates that ECE-2 is a phosphoramidon-sensitive metal protease and very similar to endothelin-1 converting enzyme (ECE-1) from endothelial cells.