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• W2040595488 abstract "Oligopeptidase B (OpdB) from Trypanosoma brucei is a candidate therapeutic target in African trypanosomiasis. OpdB is an atypical serine peptidase, since activity is inhibited by thiol‐blocking reagents and enhanced by reducing agents. We have identified C256 as the reactive cysteine residue that mediates OpdB inhibition by N ‐ethylmaleimide and iodoacetic acid. Modeling studies suggest that C256 adducts occlude the P 1 substrate‐binding site, preventing substrate binding. We further demonstrate that C559 and C597 are responsible for the thiol‐enhancement of OpdB activity. These studies may facilitate the development of specific OpdB inhibitors with therapeutic potential, by exploiting these unique properties of this enzyme." @default.
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• W2040595488 date "2005-03-17" @default.
• W2040595488 modified "2023-10-17" @default.
• W2040595488 title "Identification of the reactive cysteine residues in oligopeptidase B from<i>Trypanosoma brucei</i>" @default.
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• W2040595488 doi "https://doi.org/10.1016/j.febslet.2005.03.014" @default.
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