2-haloacid halidohydrolase [ambiguous][ambiguous]
ASB 8(aspartic acid-4-carboxymethyl ester)
Site-directed mutagenesis of the 2-haloalkanoic acid dehalogenase I gene from Pseudomonas sp. strain CBS3 and its effect on catalytic activity.
Reconsideration of the essential role of a histidine residue of L-2-halo acid dehalogenase.
Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino acid residues.
Crystallization and preliminary X-ray analysis of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10.
Improved catalytic performance of a 2-haloacid dehalogenase from Azotobacter sp. by ion-exchange immobilisation.
Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold.
Crystallization and preliminary x-ray crystallographic studies of L-2-haloacid dehalogenase from Pseudomonas sp. YL.
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) AND REVISION TO 84
Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate.
X-ray structure of a reaction intermediate of L-2-haloacid dehalogenase with L-2-chloropropionamide.
Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism.
Identification of the Mg2+-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY.
Dehalogenases applied to industrial-scale biocatalysis.
Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase.
Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase.
Identification of the dimerization domain of dehalogenase IVa of Burkholderia cepacia MBA4.
Novel catalytic mechanism of nucleophilic substitution by asparagine residue involving cyanoalanine intermediate revealed by mass spectrometric monitoring of an enzyme reaction.
MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases.
X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily.
Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily.
The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold.
According to the literature [8], [10] & [13], the catalytic reaction proceeds as follows: (1) Asp8 (of 1aq6) acts as a nucleophile, which makes a nucleophilic attack on the carbon, which is covalently bonded to halide atom, whereas Arg39 stabilizes and accepts the leaving halide atom. (The reaction proceeds via SN2 mechanism.) (2) The intermediate is stabilized by an oxyanion hole, composed of Thr12/Ser173/Asn173 in the case of R=CH3 or larger alkyl group for the substrate, or Lys147 in the case of R=H for the substrate (see [10]). (substrate; R-CX-COOH) (3) Lys147 and Tyr153 probably modulate the activity of Asp176, by lowering its pKa. (4) Asp176 acts as a base, to activate a water. (The activated water might be stabilized by Asn173 (see [10] & [16].) (5) The activated water makes a nucleophilic attack on the carbonyl carbon of Asp8-ligand intermediate, to complete the hydrolytic reaction.