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Angiotensin converting enzyme (ACE) was already discovered in insects in 1994, but its physiological role is still enigmatic. We have addressed this problem by purifying four new ACE substrates from the ovaries of the grey fleshfly, Neobellieria bullata. Their primary structures were identified as NKLKPSQWISLSD (Neb-ODAIF-11)13), NKLKPSQWI (Neb-ODAIF-11)9), SLKPSNWLTPSE (Neb-ODAIF-2) and LEQIYHL. Database analysis showed significant homology with amino acid sequence stretches as present in the N-terminal part of several fly yolk proteins | Eur. J. Biochem. 269 3522-3530 2002 FEBS 2002 doi 10.1046 j.1432-1033.2002.03043.x Characterization of four substrates emphasizes kinetic similarity between insect and human C-domain angiotensin-converting enzyme Korneel Hens1 Anick Vandingenen1 Nathalie Macours1 Geert Baggerman1 Adriana Carmona Karaoglanovic2 Liliane Schoofs1 Arnold De Loof1 and Roger Huybrechts1 1Zoological Institute of the Catholic University of Leuven Laboratory of Developmental Physiology and Molecular Biology Leuven Belgium 2Universidade Federal de Sao Paulo Escola Paulista de Medicina Department of Biophysics Sao Paulo Brazil Angiotensin converting enzyme ACE was already discovered in insects in 1994 but its physiological role is still enigmatic. We have addressed this problem by purifying four new ACE substrates from the ovaries of the grey fleshfly Neobellieria bullata. Their primary structures were identified as NKLKPSQWISLSD Neb-ODAIF-11_13 NKLKPSQWI Neb-ODAIF-11 9 SLKPSNWlTpsE Neb-ODAIF-2 and LEQIYHL. Database analysis showed significant homology with amino acid sequence stretches as present in the N-terminal part of several fly yolk proteins. An antiserum raised against Neb-ODAIF-11 9 immunostained one out of three yolk protein bands of SDS PAGE-separ-ated fly haemolymph and egg homogenate thus confirming that these peptides originate from a yolk protein gene product. Kinetic analysis of these peptides and of the peptides Neb-ODAIF and Neb-ODAIF-11 7 with insect ACE and human ACE show both similar and unique properties for insect ACE as compared withuhman C-domain ACE. Keywords ACE kinetics domain specific substrates insect physiology reproduction. Insect ACE was first isolated from head membranes of the housefly Musca domestica in 1994 1 a long time after the discovery of its mammalian counterpart in horse plasma in 1956. Since this discovery and after cloning and purification of several insect ACEs it has become clear that insect and mammalian ACE despite of their evolutionary .
