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J Biol Chem, Vol. 273, Issue 30, 19173-19182, July 24, 1998
From the We describe the characterization, cloning, and
genetic analysis of tripeptidyl peptidase II (TPP II) from
Drosophila melanogaster. Mammalian TPP II removes
N-terminal tripeptides, has wide distribution, and has been identified
as the cholecystokinin-degrading peptidase in rat brain. Size exclusion
and ion exchange chromatography produced a 70-fold purification of dTPP
II activity from Drosophila tissue extracts. The substrate
specificity and the inhibitor sensitivity of dTPP II is comparable to
that of the human enzyme. In particular, dTPP II is sensitive to
butabindide, a specific inhibitor of the rat
cholecystokinin-inactivating activity. We isolated a 4309-base pair
dTPP II cDNA which predicts a 1354-amino acid protein.
The deduced human and Drosophila TPP II proteins
display 38% overall identity. The catalytic triad, its spacing, and
the sequences that surround it are highly conserved; the C-terminal end
of dTPP II contains a 100-amino acid insert not found in the mammalian proteins. Recombinant dTPP II displays the predicted activity following
expression in HEK cells. TPP II maps to cytological position 49F4-7;
animals deficient for this interval show reduced TPP II activity.
Characterization and Cloning of Tripeptidyl Peptidase II from the
Fruit Fly, Drosophila melanogaster
,
Department of Anatomy and Neurobiology,
Washington University School of Medicine, St. Louis, Missouri 63110 and the § Department of Veterinary Medical Chemistry,
Swedish University of Agricultural Sciences, Biomedical Center,
Box 575, 751 23 Uppsala, Sweden
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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