Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/28693
Title: Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme
Authors: Machado, MFM
Cunha, F. M.
Berti, D. A.
Heimann, A. S.
Klitzke, C. F.
Rioli, V
Oliveira, V
Ferro, E. S.
Univ Cidade São Paulo
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Ptoteimax Biotecnol LTDA
CEPID
Keywords: neurolysin
thimet oligopeptidase
intracellular peptide metabolism
phosphorylation
proteasome
peptidase
Issue Date: 13-Jan-2006
Publisher: Elsevier B.V.
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 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. (c) 2005 Elsevier Inc. All rights reserved.
URI: http://repositorio.unifesp.br/handle/11600/28693
ISSN: 0006-291X
Other Identifiers: http://dx.doi.org/10.1016/j.bbrc.2005.11.041
Appears in Collections:Em verificação - Geral

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