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haloacetate + H2O = glycolate + halide
haloacetate + H2O = glycolate + halide
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haloacetate + H2O = glycolate + halide
As105 is a catalytic site residue functioning as a nucleophil attacking the alpha-carbon atom of the substrate to displace the fluorine atom, catalytic mechanism, possibly involving an imidate as intermediate
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haloacetate + H2O = glycolate + halide
enzyme contains the conserved motif Asp-Xaa-Asp-Xaa-Thr, open reaction conformation
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haloacetate + H2O = glycolate + halide
reaction mechanism of fluoroacetate dehalogenase, overview. Asp104 serves as nucleophile to attack the alpha-carbon atom of the substrate to displace the fluorine atom leading to the formation of an ester intermediate. The ester intermediate is subsequently hydrolyzed by a water molecule activated by His271, which yields glycosylate and regenerates the carboxylate group of Asp104. The catalytic triad is formed by Asp104-His271-Asp128
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haloacetate + H2O = glycolate + halide
reaction mechanism of fluoroacetate dehalogenase, overview. Asp105 serves as nucleophile to attack the alpha-carbon atom of the substrate to displace the fluorine atom leading to the formation of an ester intermediate. The ester intermediate is subsequently hydrolyzed by a water molecule activated by His272, which yields glycosylate and regenerates the carboxylate group of Asp105
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haloacetate + H2O = glycolate + halide
the fluoroacetate dehalogenase catalyzes fluoroacetate degradation through a two step process initiated by an SN2 reaction in which the aspartate residue performs a nucleophilic attack on the carbon bonded to the fluorine; the second step is hydrolysis that releases the product as glycolate, reaction activation and mechanism, overview. The activation of this catalytic step is associated to the interaction of the halogen with residues His155, Trp156, and Tyr219 (numbering according to PDB ID 3R3U from Rhodopseudomonas palustris), which may facilitate the Calpha-F bond dissociation
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haloacetate + H2O = glycolate + halide
besides residues Arg111, Arg114, His155, Trp156, and Tyr219, the important role of residues His109, Asp134, Lys181, and His280 during the defluorination process is highlighted
haloacetate + H2O = glycolate + halide
the role of the enzyme machinery and particularly of the halogen pocket in the SN2 reaction is explored by using computational tools
haloacetate + H2O = glycolate + halide
the role of the enzyme machinery and particularly of the halogen pocket in the SN2 reaction is explored by using computational tools
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haloacetate + H2O = glycolate + halide
reaction mechanism of fluoroacetate dehalogenase, overview. Asp105 serves as nucleophile to attack the alpha-carbon atom of the substrate to displace the fluorine atom leading to the formation of an ester intermediate. The ester intermediate is subsequently hydrolyzed by a water molecule activated by His272, which yields glycosylate and regenerates the carboxylate group of Asp105
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haloacetate + H2O = glycolate + halide
As105 is a catalytic site residue functioning as a nucleophil attacking the alpha-carbon atom of the substrate to displace the fluorine atom, catalytic mechanism, possibly involving an imidate as intermediate
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