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|Title:||Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme|
Cunha, F. M.
Berti, D. A.
Heimann, A. S.
Klitzke, C. F.
Ferro, E. S.
Univ Cidade São Paulo
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Ptoteimax Biotecnol LTDA
intracellular peptide metabolism
|Citation:||Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 339, n. 2, p. 520-525, 2006.|
|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 184.108.40.206), neurolysin (EC 220.127.116.11), and angiotensin-converting enzyme (EC 18.104.22.168). 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. (c) 2005 Elsevier Inc. All rights reserved.|
|Appears in Collections:||Em verificação - Geral|
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