Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/992
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dc.contributor.authorFernandes, B.l.
dc.contributor.authorAnéas, M.a.f.
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorPalma, M.s.
dc.contributor.authorLebrun, Ivo
dc.contributor.authorPortaro, Fernanda Calheta Vieira [UNIFESP]
dc.date.accessioned2015-06-14T13:25:05Z
dc.date.available2015-06-14T13:25:05Z
dc.date.issued2000-07-01
dc.identifierhttp://dx.doi.org/10.1590/S0100-879X2000000700006
dc.identifier.citationBrazilian Journal of Medical and Biological Research. Associação Brasileira de Divulgação Científica, v. 33, n. 7, p. 765-770, 2000.
dc.identifier.issn0100-879X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/992
dc.description.abstractThe protease ZapA, secreted by Proteus mirabilis, has been considered to be a virulence factor of this opportunistic bacterium. The control of its expression requires the use of an appropriate methodology, which until now has not been developed. The present study focused on the replacement of azocasein with fluorogenic substrates, and on the definition of enzyme specificity. Eight fluorogenic substrates were tested, and the peptide Abz-Ala-Phe-Arg-Ser-Ala-Ala-Gln-EDDnp was found to be the most convenient for use as an operational substrate for ZapA. A single peptide bond (Arg-Ser) was cleaved with a Km of 4.6 µM, a k cat of 1.73 s-1, and a catalytic efficiency of 376 (mM s)-1. Another good substrate for ZapA was peptide 6 (Abz-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-EDDnp) which was cleaved at a single bond (Phe-Ser) with a Km of 13.6 µM, a k cat of 3.96 s-1 and a catalytic efficiency of 291 (mM s)-1. The properties of the amino acids flanking the scissile bonds were also evaluated, and no clear requirement for the amino acid residue at P1 was found, although the enzyme seems to have a preference for a hydrophobic residue at P2.en
dc.format.extent765-770
dc.language.isoeng
dc.publisherAssociação Brasileira de Divulgação Científica
dc.relation.ispartofBrazilian Journal of Medical and Biological Research
dc.rightsAcesso aberto
dc.subjectmetalloproteaseen
dc.subjectsubstrate specificityen
dc.subjectquenched fluorescence peptidesen
dc.subjectProteus mirabilisen
dc.titleDevelopment of an operational substrate for ZapA, a metalloprotease secreted by the bacterium Proteus mirabilisen
dc.typeArtigo
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade Estadual de São Paulo
dc.contributor.institutionInstituto Butantan
dc.description.affiliationUniversidade de São Paulo
dc.description.affiliationUniversidade Federal de São Paulo (UNIFESP)
dc.description.affiliationUniversidade Estadual de São Paulo
dc.description.affiliationInstituto Butantan
dc.description.affiliationUnifespUNIFESP
dc.identifier.fileS0100-879X2000000700006.pdf
dc.identifier.scieloS0100-879X2000000700006
dc.identifier.doi10.1590/S0100-879X2000000700006
dc.description.sourceSciELO
dc.identifier.wosWOS:000088236100006
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