EC Number |
Reaction |
Reference |
---|
3.8.1.2 | (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide |
acts on acids of short chain lengths, C2 to C4 with inversion at C2 |
- |
3.8.1.2 | (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide |
Asp10 of the enzyme functions as a catalytic nucleophile: the residue attacks the alpha-carbon of the substrate to form an ester intermediate, which is subsequently hydrolysed to release the product |
-, 648282, 648291, 648295, 648317 |
3.8.1.2 | (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide |
functional residue: Asp 10 |
648311, 648313 |
3.8.1.2 | (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide |
it is hypothesized that, in DehL, catalysis is initiated by a nucleophilic attack launched by the side-chain carboxyl of Asp13 on the C2 of L-2CP to form an ester intermediate, which is subsequently hydrolyzed by a water molecule activated by His184 followed by product release |
756515 |
3.8.1.2 | (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide |
mechanism |
-, 648282 |
3.8.1.2 | (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide |
reaction mechanism, overview |
-, 719121 |
3.8.1.2 | (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide |
structure-function analysis, catalytic mechanism, modeling. Asp181 is proposed to participate in the activation of the catalytic water molecule required for hydrolysis of the ester intermediate, Asp186 and Lys157 in DehRhb are responsible for deprotonation of the catalytic water molecule in the second part of the enzyme reaction. In DehRhb, the catalytic water molecule is coordinated by His183 and the conserved Asp186. This residue makes an ion pair with the conserved Lys157. The His183 makes an H-bond with the catalytic Asp18 on one side and an ion pair with Glu21 on the other side. This forms a catalytic triad similar to that observed in the haloalkane dehalogenases |
733826 |
3.8.1.2 | (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide |
the stereochemistry of the product obtained from racemic 2-brompropionic acid by the action of celite-immobilized disrupted cells in dimethylsulfoxid differs from that of the enantiomer obtained in an aqueous buffer |
-, 648316 |