sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014).