CareLit Fachartikel

The peptidyl-prolyl isomerase SlrA contributes to virulence and adherence of Streptococcus pneumoniae

S Hammerschmidt, PV Adrian, C Albert, S Estevão, T Hoogenboezem, IHT Luijendijk, T Kamphausen, PWM Hermans · Pneumologie · 2006 · Heft 02

Dokument
1102906
CareLit-ID
Jahr
2006
Publikation
PDF
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Metadaten
DOI
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Bibliografische Angaben

Zeitschrift
Pneumologie
Autor:innen
S Hammerschmidt, PV Adrian, C Albert, S Estevão, T Hoogenboezem, IHT Luijendijk, T Kamphausen, PWM Hermans
Ausgabe
Heft 02 / 2006
Seiten
–
Erschienen: 2006-02-08 00:00:00
ISSN
0934-8387

Zusammenfassung

Streptococcus pneumoniae expresses two lipoproteins, which resemble homology with distinct families of peptidyl-prolyl isomerases (PPIases). The PpmA protein is homologous with the parvulin family of PPIases, whereas the streptococcal lipoprotein rotamase A (SlrA) resembles homology with the cyclophilins. In this study, we investigated the PPIase activity of SlrA and PpmA, and in particular the contribution of SlrA to virulence. SlrA clearly displayed PPIase activity, whereas PpmA did not show detectable PPIase activity. With respect to substrate specificity of SlrA, the largest kcat/KM was determined for the al…

Schlagworte

Cyclophilins Alanine Pneumologie