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PMID:7775412
| Citation |
Cornell, MJ, Williams, TA, Lamango, NS, Coates, D, Corvol, P, Soubrier, F, Hoheisel, J, Lehrach, H and Isaac, RE (1995) Cloning and expression of an evolutionary conserved single-domain angiotensin converting enzyme from Drosophila melanogaster. J. Biol. Chem. 270:13613-9 |
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| Abstract |
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 (Km, 365 microM), removes Phe-Arg from the C terminus of bradykinin (Km, 22 microM), and is inhibited by ACE inhibitors, captopril (IC50 = 1.1 x 10(-9) M) and trandolaprilat (IC50 = 1.6 x 10(-8) M). 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 (IC50 = 5.6 x 10(-9) M) and trandolaprilat (IC50 = 2 x 10(-8) M). The evolutionary significance of these results is discussed. |
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| Keywords |
Amino Acid Sequence; Animals; Base Sequence; Biological Evolution; Cells, Cultured; Cloning, Molecular; Conserved Sequence; Drosophila melanogaster/enzymology; Molecular Sequence Data; Peptidyl-Dipeptidase A/chemistry; Peptidyl-Dipeptidase A/genetics; Peptidyl-Dipeptidase A/isolation & purification; Recombinant Proteins/biosynthesis |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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