ECE2 cleaves EDN1(53-90)

Stable Identifier
Reaction [transition]
Homo sapiens
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Endothelin-converting enzyme 2 (ECE2) belongs to the type II membrane-bound zinc metalloprotease family and shares 59% sequence similarity to ECE1 (Emoto & Yanagisawa1995, Yanagisawa et al. 2000, Lorenzo et al. 2001). In contrast to ECE1, the optimum pH for ECE2 activity is acidic (pH 5.5), which would favor an intracellular localization and a potential role under low pH conditions, for example in ischemia. This difference provides an experimental method for distinguishing between the activities of the two enzymes. ECE2 was found to be localized to the acidified environment of vesicles of the secretory pathway in human endothelial cells but was not detected in Weibel-Palade storage granules (Russell & Davenport 1999).

Literature References
PubMed ID Title Journal Year
7797512 Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum

Emoto, N, Yanagisawa, M

J. Biol. Chem. 1995
Catalyst Activity

metalloendopeptidase activity of ECE2 [transport vesicle membrane]

Orthologous Events
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