ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity
Braz. j. med. biol. res
;
34(11): 1397-1403, Nov. 2001. ilus, tab
Artículo
en Inglés
| LILACS, SES-SP
| ID: lil-303314
ABSTRACT
The opportunistic bacterium Proteus mirabilis secretes a metalloprotease, ZapA, considered to be one of its virulence factors due to its IgA-degrading activity. However, the substrate specificity of this enzyme has not yet been fully characterized. In the present study we used fluorescent peptides derived from bioactive peptides and the oxidized ß-chain of insulin to determine the enzyme specificity. The bradykinin- and dynorphin-derived peptides were cleaved at the single bonds Phe-Ser and Phe-Leu, with catalytic efficiencies of 291 and 13 mM/s, respectively. Besides confirming already published cleavage sites, a novel cleavage site was determined for the ß-chain of insulin (Val-Asn). Both the natural and the recombinant enzyme displayed the same broad specificity, demonstrated by the presence of hydrophobic, hydrophilic, charged and uncharged amino acid residues at the scissile bonds. Native IgA, however, was resistant to hydrolysis by ZapA
Texto completo:
Disponible
Índice:
LILACS (Américas)
Asunto principal:
Proteus mirabilis
/
Proteínas Bacterianas
/
Metaloendopeptidasas
Idioma:
Inglés
Revista:
Braz. j. med. biol. res
Año:
2001
Tipo del documento:
Artículo
Institución/País de afiliación:
Instituto Butantan/BR
/
Universidade Estadual Paulista/BR
/
Universidade Federal de Säo Paulo/BR
/
Universidade de Säo Paulo/BR
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