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dc.contributor.authorJudice, Wagner AS
dc.contributor.authorPuzer, Luciano
dc.contributor.authorCotrin, Simone Silva [UNIFESP]
dc.contributor.authorCarmona, Adriana Karaoglanovic [UNIFESP]
dc.contributor.authorCoombs, Graham H.
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorJuliano, Maria Aparecida [UNIFESP]
dc.date.accessioned2016-01-24T12:34:18Z
dc.date.available2016-01-24T12:34:18Z
dc.date.issued2004-03-01
dc.identifierhttp://dx.doi.org/10.1111/j.1432-1033.2004.04008.x
dc.identifier.citationEuropean Journal of Biochemistry. Oxford: Blackwell Publishing Ltd, v. 271, n. 5, p. 1046-1053, 2004.
dc.identifier.issn0014-2956
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/27639
dc.description.abstractThe recombinant cysteine peptidases, cruzain from Trypanosoma cruzi and CPB2.8DeltaCTE from Leishmania mexicana, are cathepsin L-like and characteristically endopeptidases. in this study, we characterized the carboxydipeptidase activities of these enzymes and compared them with those of human recombinant cathepsin B and cathepsin L. the analysis used the internally quenched fluorescent peptide Abz-FRFK*-OH and some of its analogues, where Abz is ortho-aminobenzoic acid and K* is (2,4-dinitrophenyl)-epsilon-NH2-lysine. These peptides were demonstrated to be very sensitive substrates, due to the strong quenching effect of K* on the fluorescence of the Abz group. the carboxydipeptidase activity of cruzain was shown to be very similar to that of cathepsin B, while that of CPB2.8DeltaCTE is closer to the carboxydipeptidase activity of cathepsin L. the S-2 subsite architecture of cruzain and the nature of the amino acid at the P-2 position of the substrates determine its carboxydipeptidase activity and gives further and direct support to the notion that the carboxydipeptidase activity of the papain family cysteine peptidases rely on the S-2-P-2 interaction [Nagler D. K., Tam, W., Storer, A.C., Krupa, J.C., Mort, J.S. & Menard, R. (1999) Biochemistry38, 4868-4874]. Cruzain and CPB2.8DeltaCTE presented a broad pH-range for both the endo- and exo-peptidase activities, although the later is approximately one order of magnitude lower. This feature, that is not common in related mammalian cysteine peptidases, is consistent with the enzymes being exposed to different environmental conditions and having different locations during parasite development.en
dc.format.extent1046-1053
dc.language.isoeng
dc.publisherBlackwell Publishing Ltd
dc.relation.ispartofEuropean Journal of Biochemistry
dc.rightsAcesso aberto
dc.subjectcathepsin Ben
dc.subjectcathepsin Len
dc.subjectcruzipainen
dc.subjectexoproteasesen
dc.subjectproteasesen
dc.titleCarboxydipeptidase activities of recombinant cysteine peptidases - Cruzain of Trypanosoma cruzi and CPB of Leishmania mexicanaen
dc.typeArtigo
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Glasgow
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-0404420 São Paulo, Brazil
dc.description.affiliationUniv Glasgow, Inst Biomed & Life Sci, Div Infect & Immun, Glasgow G12 8QQ, Lanark, Scotland
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-0404420 São Paulo, Brazil
dc.identifier.doi10.1111/j.1432-1033.2004.04008.x
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000189052600016


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