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Results 1 - 5 of 5
EC Number
Inhibitors
Commentary
Structure
3,4-dichloroisocoumarin
mechanism-based inactivation
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anti-factor D Fab fragment
an Escherichia coli-expressed, humanized Fab fragment, derived from monoclonal antibody 166-32, and designed as specific enzyme inhibitor targeting the exosite. Anti-factor D Fab fragment prevents factor D-mediated proteolytic activation of its macromolecular substrate C3bB, but not proteolysis of a small synthetic substrate, indicating that the inhibitor does not block access of the substrate to the catalytic site, binding structure and inhibitory mechanism, overview. The structures show that the AFD-binding site includes surface loops of the enzyme that form part of the enzyme's exosite. Anti-factor D Fab fragment inhibits the enzyme proteolytic function by interfering with macromolecular substrate access rather than by inhibiting the enzyme catalysis
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diisopropyl fluorophosphate
-
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isatoic anhydride
-
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more
human factor D is a self-inhibited thrombin-like serine proteinase. Ser199 of the self-inhibitory loop blocks the formation of the canonical active configurations
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Results 1 - 5 of 5