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Volume 270, Number 23, Issue of June 9, pp. 13613-13619, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Michael J. Cornell , Tracy A.Williams , Nazarius S. Lamango , David Coates , Pierre Corvol , Florent Soubrier , Jorg Hoheisel , Hans Lehrach , R. Elwyn Isaac

Mammalian somatic angiotensin converting enzyme (EC 3.4.15.1, ACE) consists of two highly homologous (N- and C-) domains encoded by a duplicated gene. We have identified an apparent single-domain (67 kDa) insect angiotensin converting enzyme (AnCE) in embryos of Drosophila melanogaster which converts angiotensin I to angiotensin II (K, 365 µM), removes Phe-Arg from the C terminus of bradykinin (K, 22 µM), and is inhibited by ACE inhibitors, captopril (IC = 1.1 10M) and trandolaprilat (IC = 1.6 10M). We also report the cloning and expression of a Drosophila AnCE cDNA which codes for a single-domain 615-amino acid protein with a predicted 17-amino acid signal peptide and regions with high levels of homology to both the N- and C-domains of mammalian somatic ACE, especially around the active site consensus sequence. Northern analysis identified a single 2.1-kilobase mRNA in Drosophila embryos, and Southern analysis of Drosophila genomic DNA indicates that the insect gene is not duplicated. When expressed in COS-7 cells, the AnCE protein is a secreted enzyme, which converts angiotensin I to angiotensin II and is inhibited by captopril (IC = 5.6 10M) and trandolaprilat (IC = 2 10M). The evolutionary significance of these results is discussed.

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