Selected article for: "active site and catalytic cysteine"
Author: Kuban-Jankowska, Alicja; Sahu, Kamlesh K; Niedzialkowski, Pawel; Gorska, Magdalena; Tuszynski, Jack A; Ossowski, Tadeusz; Wozniak, Michal
Title: Redox process is crucial for inhibitory properties of aurintricarboxylic acid against activity of YopH: virulence factor of Yersinia pestis
  • Document date: 2015_7_22
    • ID: 1irvzt8v_35
    Snippet: The reduction assay indicated that ATA is a reversible inhibitor of YopH and that the presence of catalase abolished the effect of ATA on YopH. The inactivation of the inhibitory activity of the compound in the presence of catalase is likely through an oxidative mechanism, due to the fact that catalase is an enzyme protecting cells from reactive oxygen species by decomposition of hydrogen peroxide [22] . Some of the PTP inhibitors are acting by p.....
    Document: The reduction assay indicated that ATA is a reversible inhibitor of YopH and that the presence of catalase abolished the effect of ATA on YopH. The inactivation of the inhibitory activity of the compound in the presence of catalase is likely through an oxidative mechanism, due to the fact that catalase is an enzyme protecting cells from reactive oxygen species by decomposition of hydrogen peroxide [22] . Some of the PTP inhibitors are acting by production of hydrogen peroxide, which is suggested as a key regulator of PTP activity in cells [23] . ATA loses the inhibitory properties against PTPs in the presence of catalase, which shows that the mechanism of ATA induced inactivation of YopH is probably involved with the oxidation of catalytic cysteine in an active site. It is confirmed also by the loss of unoxidized thiol groups in YopH after treatment with ATA.

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