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Peptidyl dipeptidases (Ance and Acer) of Drosophila melanogaster: major differences in the substrate specificity of two homologs of human angiotensin I-converting enzyme.

Siviter, Richard J. and Nachman, Ronald J. and Dani, M. Paulina and Keen, Jeffrey N. and Shirras, Alan D. and Isaac, R. Elwyn (2002) Peptidyl dipeptidases (Ance and Acer) of Drosophila melanogaster: major differences in the substrate specificity of two homologs of human angiotensin I-converting enzyme. Peptides, 23 (11). pp. 2025-2034. ISSN 0196-9781

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Abstract

Drosophila melanogaster angiotensin converting enzyme (Ance) and angiotensin converting enzyme related (Acer) are single domain homologs of mammalian peptidyl dipeptidase A (angiotensin I-converting enzyme) whose physiological substrates have not as yet been identified. We have investigated the in vitro substrate specificities of the two peptidases towards a variety of insect and mammalian peptides. Ance was generally much better than Acer at hydrolyzing peptides of 5–13 amino acids in length. Only two of the peptides, [Leu5]enkephalinamide and leucokinin-I were cleaved faster by Acer. Increasing NaCl concentration had opposite affects on the cleavage of [Leu5]enkephalin and [Leu5]enkephalinamide by Acer, decreasing the activity towards [Leu5]enkephalin but increasing the activity towards [Leu5]enkephalinamide. Of the insect peptides tested, the tachykinin-related peptide, Lom TK-1, proved to be the best substrate for Ance with a kcat/Km ratio of 0.122 s−1 μM−1. However, in comparison, the D. melanogaster tachykinins, DTK-1, DTK-2, DTK-3 and DTK-4 were poor Ance substrates. DTK-5 was the best substrate of this family, but the apparent high Km for hydrolysis by Ance suggested that this peptide would not be a natural Ance substrate. This low affinity for DTK-5 is the likely reason why the peptide was not rapidly degraded in D. melanogaster hemolymph, where Ance was shown to be a major peptide-degrading activity.

Item Type: Article
Journal or Publication Title: Peptides
Uncontrolled Keywords: Insect tachykinin ; Insect peptides ; Peptide metabolism ; Peptidases ; Tachykinin-related peptides
Subjects: Q Science > QH Natural history > QH301 Biology
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 9378
Deposited By: Dr Alan Shirras
Deposited On: 05 Jun 2008 16:54
Refereed?: Yes
Published?: Published
Last Modified: 26 Jul 2012 18:36
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/9378

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