Angiotensin converting enzyme. Domain structure and properties Kugaevskaya E.V.1 1. V. N. Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences (RAMS) Section: Review PubMed Id: 16521820
Year: 2005 Volume: 51 Issue : 6 Pages: 567-580in vivo the natural peptide (N-AcSer-Asp-Lys-Pro), a negative regulator of hematopoietic stem cell proliferation. Somatic ACE is a single-chain glycoprotein, which contains two highly homologous domains (N- and C-domains, respectively), possessing a zinc-dependent active site. The domains differ in the rate of substrate hydrolysis, interaction with ACE inhibitors and chloride activation profiles. Specific ACE inhibitors used for treatment of hypertension, inhibit both domains, but their dissociation rates of enzyme-inhibitor complex are different. Selective binding of ACE inhibitors to either N- or C-domain may influence their biological effect during treatment. Different functional significance of these domains may be due to some differences in their three-dimentional structures. X-ray structure of testicular ACE was recently solved and three-dimentional structure of N-domain was modeled. The structural features of domain active sites may be useful for construction of new selective inhibitors. Download PDF: Keywords: angiotensin-converting enzyme, domains, structure, inhibitors
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Kugaevskaya E.V. (2005) Angiotensin converting enzyme. Domain structure and properties. Biomeditsinskaya Khimiya, 51 (6), 567-580.
et al. Angiotensin converting enzyme. Domain structure and properties // Biomeditsinskaya Khimiya. - 2005. - V. 51. -N 6. - P. 567-580.
et al., "Angiotensin converting enzyme. Domain structure and properties." Biomeditsinskaya Khimiya 51.6 (2005): 567-580.
Kugaevskaya, , E. V. (2005). Angiotensin converting enzyme. Domain structure and properties. Biomeditsinskaya Khimiya , 51(6), 567-580.
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