Biochemical characterization of endothelin converting enzyme

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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.