Background: Development of small potent synthetic inhibitors of Clostridium botulinum neurotoxin A remains an unresolved challenge. Results: Small compounds incorporating electrophile moiety can block enzyme activity by covalent modification of Cys 165 . Conclusion: A structural framework for developing potent covalent inhibitors of Clostridium botulinum neurotoxin A is provided. Significance: This study uncovers a subfamily of zinc proteases containing a conserved cysteine in their active site.
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