Analysis of oligopeptidase activity in Ndel1 conditional knockout mice
Search for new substrates and / or inhibitors for EP24.15 and EP24.16 in the low m...
| Full text | |
| Author(s): |
Machado, M. F. M.
;
Cunha, F. M.
;
Berti, D. A.
;
Heimann, A. S.
;
Klitzke, C. F.
;
Rioli, V.
;
Oliveira, V.
;
Ferro, E. S.
[8]
Total Authors: 8
|
| Document type: | Journal article |
| Source: | Biochemical and Biophysical Research Communications; v. 339, n. 2, p. 518-523, Jan. 2006. |
| Field of knowledge: | Biological Sciences - Morphology |
| Abstract | |
Recent findings from our laboratory suggest that intracellular peptides containing putative post-translational modification sites (i.e., phosphorylation) could regulate specific protein interactions. Here, we extend our previous observations showing that peptide phosphorylation changes the kinetic parameters of structurally related endopeptidase EP24.15 (EC 3.4.24.15), neurolysin (EC 3.4.24.16), and angiotensin-converting enzyme (EC 3.4.15.1). Phosphorylation of peptides that are degraded by these enzymes leads to reduced degradation, whereas phosphorylation of peptides that interacted as competitive inhibitors of these enzymes alters only the K-i's. These data suggest that substrate phosphorylation could be one of the mechanisms whereby some intracellular peptides would escape degradation and could be regulating protein interactions within cells. (AU) | |
| FAPESP's process: | 04/04933-2 - Molecular cell biology of oligopeptidases |
| Grantee: | Emer Suavinho Ferro |
| Support Opportunities: | Research Projects - Thematic Grants |