EC Number   |
General Information |
Reference |
|---|
   3.8.1.3 | more |
density functional theory calculations of the SN2 initiation reaction modeled through the interaction between the substrate and the propionate anion as the nucleophile, the reaction energy is modulated by the degree of stabilization of the fluoride anion formed after the SN2 reaction. The activation of this catalytic step is associated to the interaction of the halogen with residues His155, Trp156, and Tyr219, which may facilitate the Calpha-F bond dissociation |
734366 |
| 3.8.1.3 | more |
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 |
719121 |
| 3.8.1.3 | more |
the enzyme active site is composed of Asp104, Arg105, Arg108, His149, Trp150, Tyr212, and His271, environments of the tryptophan residues are different between the fluoroacetate and chloroacetate-bound enzymes, active site docking simulations and QM/MM optimizations, QM/MM calculations for the defluorination of fluoroacetate, overview |
719300 |
| 3.8.1.3 | physiological function |
fluoroacetate dehalogenase catalyzes degradation of the environmentally toxic fluoroacetate 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 |
734366 |
| 3.8.1.3 | physiological function |
the degradation of haloacid is mediated by the production of the inducible dehalogenase. Presence of distinct inducible acetate- and monochloroacetate-transport system in MBA4. Determination of relative acetate- and monochloroacetate-uptake activities of MBA4 grown in various substrates and inhibition of acetate- and monochloroacetate-uptake by other solutes, overview |
-, 733578 |
