A study of chimeras constructed with the two domains of angiotensin I-converting enzyme

Article abstract of DOI:10.1016/0006-2952(95)02125-6

Angiotensin I-converting enzyme (ACE) is composed of two highly similar domains called the N and C domains, which display some contrasting enzymatic properties. We constructed two ACE chimeras: chimera 1, comprised of the N domain containing the central 60 amino acid residues of the C domain, and chimera 2, comprised of the C domain containing the central 60 amino acid residues of the N domain. Chimeras 1 and 2 displayed K(m) values for Hip-His-Leu and Z-Phe-His-Leu and k(cat) ratios for these two substrates similar to that of the N and C domains, respectively. Thus, the short sequence exchanged between the two domains does not confer the specific properties of that domain for these two substrates but, rather, such specific properties must arise from the sequences surrounding the central region in each domain.