A study of chimeras constructed with the two domains of angiotensin I-converting enzyme.
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 Km values for Hip-His-Leu and Z-Phe-His-Leu and kcat 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.
INSERM Unité 36, Paris, France.
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Williams
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Danilov
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Alhenc-Gelas
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Soubrier
D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D007703:Peptidyl-Dipeptidase A / Q000235:genetics*; D011993:Recombinant Fusion Proteins; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D009842:Oligopeptides; D011993:Recombinant Fusion Proteins; D007703:Peptidyl-Dipeptidase A