A proposed role for Leishmania major carboxypeptidase in peptide catabolism
Resource
Biochemical and Biophysical Research Communications, 373(1), 25-29
Journal
Biochemical and Biophysical Research Communications
Pages
25-29
Date Issued
2008
Date
2008
Author(s)
Isaza, C. E.
Zhong , X. J.
Rosas, L. E.
White, J. D.
Chen, R. P. Y.
Liang, G. F. C.
Chan, S. I.
Satoskard, A. R.
Chan, M. K.
Abstract
Leishmaniasis is a tropical disease caused by Leishmania, eukaryotic parasites transmitted to humans by sand flies. Towards the development of new chemotherapeutic targets for this disease, biochemical and in vivo expression studies were performed on one of two M32 carboxypeptidases present within the Leishmania major (LmaCP1) genome. Enzymatic studies reveal that like previously studied M32 carboxypeptidases, LmaCP1 cleaves substrates with a variety of C-terminal amino acids--the primary exception being those having C-terminal acidic residues. Cleavage assays with a series of FRET-based peptides suggest that LmaCP1 exhibits a substrate length restriction, preferring peptides shorter than 9-12 amino acids. The in vivo expression of LmaCP1 was analyzed for each major stage of the L. major life cycle. These studies reveal that LmaCP1 expression occurs only in procyclic promastigotes--the stage of life where the organism resides in the abdominal midgut of the insect. The implications of these results are discussed.
SDGs
Type
journal article
File(s)![Thumbnail Image]()
Loading...
Name
07.pdf
Size
23.21 KB
Format
Adobe PDF
Checksum
(MD5):1654e9d69a3006b1fd80450abdb8b1b1