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Literature summary for 3.8.1.3 extracted from

  • Kurihara, T.
    A mechanistic analysis of enzymatic degradation of organohalogen compounds (2011), Biosci. Biotechnol. Biochem., 75, 189-198.
    View publication on PubMed
Search for more literature for 3.8.1.3

Organism

Organism UniProt Comment Textmining
Burkholderia sp.
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-
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Delftia acidovorans
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-
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Delftia acidovorans B
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-
-

Reaction

Reaction Comment Organism Reaction ID
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 Burkholderia sp.
a
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 Delftia acidovorans
a

Synonyms

Synonyms Comment Organism
FAc-Dex FA1
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 Burkholderia sp.
FAc-Dex H1
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 Delftia acidovorans
fluoroacetate dehalogenase
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 Delftia acidovorans
fluoroacetate dehalogenase
-
 Burkholderia sp.

General Information

General Information Comment Organism
additional information the active site is formed by Phe34, Asp104, Arg105, Arg108, Asp128, His271, and Phe272 of the core domain, as well as of Tyr147, His149, Trp150, and Tyr212 of the cap domain, structure analysis, overview Burkholderia sp.