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dc.contributor.authorCamargo, Antonio Carlos Martins de [UNIFESP]
dc.contributor.authorGomes, Marcelo Damario [UNIFESP]
dc.contributor.authorReichl, Antonia P.
dc.contributor.authorFerro, Emer Suavinho [UNIFESP]
dc.contributor.authorJacchieri, Saul
dc.contributor.authorHirata, Izaura Yoshico [UNIFESP]
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.date.accessioned2018-06-15T14:04:22Z
dc.date.available2018-06-15T14:04:22Z
dc.date.issued1997-06-01
dc.identifierhttp://dx.doi.org/10.1042/bj3240517
dc.identifier.citationBiochemical Journal. London: Portland Press, v. 324, n. 2, p. 517-522, 1997.
dc.identifier.issn0264-6021
dc.identifier.urihttp://repositorio.unifesp.br/11600/42801
dc.description.abstractA systematic analysis of the peptide sequences and lengths of several homologues of bioactive peptides and of a number of quenched-fluorescence (qf) opioid- and bradykinin-related peptides was performed to determine the main features leading the oligopeptides to hydrolysis by the recombinant rat testis thimet oligopeptidase (EC 3.4.24.15). The results indicate that a minimum substrate length of six amino acids is required and that among the oligopeptides six to thirteen amino acid residues long, their susceptibility as substrates is highly variable. Thimet oligopeptidase was able to hydrolyse, with similar catalytic efficiency, peptide bonds having hydrophobic or hydrophilic amino acids as well as proline in the P1 position of peptides, ranging from a minimum of six to a maximum of approximately thirteen amino acid residues. An intriguing observation was the shift of the cleavage site, at a Leu-Arg bond in qf dynorphin (2-8) [qf-Dyn(2-8); Abz-GGFLRRV-EDDnp, where Abz stands for o-aminobenzoyl and EDDnp for N-(2,4-dinitrophenyl) ethylenediamine], to Arg-Arg in qf-Dyn(2-8)Q, in which Gln was substituted for Val at its C-terminus. Similarly, a cleavage site displacement was also observed with the hydrolysis of the internally quenched-fluorescence bradykinin analogues containing Gin at the C-terminal position, namely Abz-RPPGFSPFR-EDDnp and Abz-GFSPFR-EDDnp are cleaved at the Phe-Ser bond, but Abz-RPPGFSPFRQ-EDDnp and Abz-GFSPFRQ-EDDnp are cleaved at the Pro-Phe bond.en
dc.format.extent517-522
dc.language.isoeng
dc.publisherPortland Press
dc.relation.ispartofBiochemical Journal
dc.rightsAcesso aberto
dc.titleStructural features that make oligopeptides susceptible substrates for hydrolysis by recombinant thimet oligopeptidaseen
dc.typeArtigo
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionINST BUTANTAN
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionFDN ANTONIO PRUDENTE
dc.description.affiliationUNIV FED SAO PAULO,ESCOLA PAULISTA MED,DEPT BIOFIS,BR-04044020 SAO PAULO,SP,BRAZIL
dc.description.affiliationINST BUTANTAN,BIOCHEM & BIOPHYS LAB,BR-05503900 SAO PAULO,BRAZIL
dc.description.affiliationUNIV SAO PAULO,INST BIOMED SCI,SAO PAULO,BRAZIL
dc.description.affiliationFDN ANTONIO PRUDENTE,BR-01509010 SAO PAULO,BRAZIL
dc.description.affiliationUnifespUNIV FED SAO PAULO,ESCOLA PAULISTA MED,DEPT BIOFIS,BR-04044020 SAO PAULO,SP,BRAZIL
dc.identifier.doi10.1042/bj3240517
dc.description.sourceWeb of Science
dc.identifier.wosWOS:A1997XD37700023


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