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Fluoroacetate dehalogenase : ウィキペディア英語版 | Fluoroacetate dehalogenase
Fluoroacetate dehalogenase catalyzes the hydrolytic defluorination of the toxic fluoroacetate to produce glycolate. This enzyme is unique in that it catalyzes the cleavage of a strong carbon–fluorine bond of an aliphatic compound. The enzyme also acts on chloroacetate, although much less efficiently. The enzyme belongs to the hydrolase superfamily (one of the largest known enzyme families comprising approximately 1% of the genes in the human genome) and exists as a homodimer.
==Reactions== Fluoroacetate dehalogenase is unique because it catalyzes the cleavage of the remarkably stable carbon–fluorine bond of a fluorinated aliphatic compound. In the reaction of L-2-haloacid dehalogenase and fluoroacetate dehalogenase, the carboxylate group performs a nucleophilic attack on the alpha-carbon atom, moving the halogen atom. This action is common to haloalkane dehalogenase and 4-chlorobenzoyl-CoA dehalogenase. DL-2-Haloacid dehalogenase is unique in that a water molecule directly attacks the substrate, displacing the halogen atom.
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