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- W1967448217 abstract "Arg‐gingipain B (RgpB), a major virulence factor secreted by the periodontal pathogen Porphyromonas gingivalis is an Arg‐specific cysteine proteinase. By monitoring proteolytic cleavage of a human salivary peptide histatin 5 using MALDI‐TOF MS, RgpB purified from P. gingivalis HG66 was found to shift from a dominant Arg‐X to dominant Lys‐X activity, both in vitro and in vivo, upon reversible cysteine oxidation. Native PAGE analysis revealed the association of novel Lys‐X activity with a reversible state change of the oxidized enzyme. The redox‐regulated Lys‐X activity of RgpB may provide a survival advantage to P. gingivalis against the oxidative host defence." @default.
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- W1967448217 date "2013-03-13" @default.
- W1967448217 modified "2023-09-27" @default.
- W1967448217 title "Reversible redox regulation of specificity of Arg‐gingipain B in <i>Porphyromonas gingivalis</i>" @default.
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- W1967448217 doi "https://doi.org/10.1016/j.febslet.2013.02.051" @default.
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