Endothelin-converting enzyme (ECE) 

Endothelin-Converting Enzyme (ECE) belongs to the M13 family of zinc metalloproteases and is a membrane-bound endopeptidase. ECE preferentially cleaves on the amino side of hydrophobic amino acid residues, with the ability to precisely hydrolyze a series of biologically inactive intermediates known as big endothelins (big ET-1, -2, and -3) at the Trp21-Val/Ile22 bond, thereby forming biologically active endothelin-1 (ET-1), endothelin-2 (ET-2), and endothelin-3 (ET-3). These endothelins play a pivotal role in blood flow regulation.
The ECE family comprises three members: ECE-1, ECE-2, and ECE-3, each encoded by a distinct gene. Unlike other family members, ECE-3 (also known as the Kell blood group antigen) is predominantly found in red blood cell tissue and is not expressed in the central nervous system (CNS).
ECE is commonly used in research on cardiovascular diseases (such as hypertension) and Alzheimer's disease^[1][2].

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