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Literature summary extracted from

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

Application

EC Number Application Comment Organism
1.3.1.103 synthesis the enzyme is useful in the production of L-2-chloropropionate, a building block in the synthesis of aryloxyphenoxypropionate herbicides Burkholderia sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.8.1.2 mutant S175A in complex with chloroacetate, 2-L-chlorobutyrate, 2-L-chloro-3-methylbutyrate, 2-L-chloro-4-methylvalerate, and L-2-chloropropionamide, all substrates bound have D-configuration, except for chloroacetate Pseudomonas sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.8.1.2 D180A site-directed mutagenesis of a residue that strongly interacts with the substrate Pseudomonas sp.
3.8.1.2 K151A site-directed mutagenesis of a residue that strongly interacts with the substrate Pseudomonas sp.
3.8.1.2 S175A site-directed mutagenesis of a residue that strongly interacts with the substrate Pseudomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.103 2-bromoacrylate + NADPH + H+ Burkholderia sp. no activity with NADH (S)-2-bromopropanoate + NADP+
-
 ?
1.3.1.103 2-chloroacrylate + NADPH + H+ Burkholderia sp.
-
 (S)-2-chloropropanoate + NADP+
-
 ?
3.8.1.2 (S)-2-chloropropionic acid + H2O Pseudomonas sp.
-
 (R)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.2 (S)-2-chloropropionic acid + H2O Pseudomonas sp. 113
-
 (R)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.10 (R)-2-chloropropionic acid + H2O Pseudomonas sp.
-
 (S)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.10 (R)-2-chloropropionic acid + H2O Pseudomonas sp. 113
-
 (S)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.10 (S)-2-chloropropionic acid + H2O Pseudomonas sp.
-
 (R)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.10 (S)-2-chloropropionic acid + H2O Pseudomonas sp. 113
-
 (R)-2-hydroxypropionic acid + chloride
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.103 Burkholderia sp. Q59I44
-
-
3.8.1.2 Pseudomonas sp.
-
-
-
3.8.1.3 Burkholderia sp.
-
-
-
3.8.1.3 Delftia acidovorans
-
-
-
3.8.1.3 Delftia acidovorans B
-
-
-
3.8.1.10 Pseudomonas sp.
-
-
-
3.8.1.10 Pseudomonas sp. 113
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.8.1.2 (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide reaction mechanism, overview Pseudomonas sp.
a
3.8.1.3 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
3.8.1.3 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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.103 2-bromoacrylate + NADPH + H+ no activity with NADH Burkholderia sp. (S)-2-bromopropanoate + NADP+
-
 ?
1.3.1.103 2-chloroacrylate + NADPH + H+
-
 Burkholderia sp. (S)-2-chloropropanoate + NADP+
-
 ?
1.3.1.103 2-chloroacrylate + NADPH + H+ no activity with NADH Burkholderia sp. (S)-2-chloropropanoate + NADP+
-
 ?
3.8.1.2 (S)-2-chloropropionic acid + H2O
-
 Pseudomonas sp. (R)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.2 (S)-2-chloropropionic acid + H2O the substrate interacts strongly with Asp10, Arg41, Lys151, and Asp180 Pseudomonas sp. (R)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.2 (S)-2-chloropropionic acid + H2O
-
 Pseudomonas sp. 113 (R)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.2 additional information the enzyme reaction mechanism proceeds via an ester intermediate and a nucleophilic aspartate attacking the C-atom of the substrate to displace the halo-atom, mass spectrometral analysis of the structural changes during catalysis, overview Pseudomonas sp. ?
-
 ?
3.8.1.2 additional information the enzyme reaction mechanism proceeds via an ester intermediate and a nucleophilic aspartate attacking the C-atom of the substrate to displace the halo-atom, mass spectrometral analysis of the structural changes during catalysis, overview Pseudomonas sp. 113 ?
-
 ?
3.8.1.10 (R)-2-chloropropionic acid + H2O
-
 Pseudomonas sp. (S)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.10 (R)-2-chloropropionic acid + H2O
-
 Pseudomonas sp. 113 (S)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.10 (S)-2-chloropropionic acid + H2O
-
 Pseudomonas sp. (R)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.10 (S)-2-chloropropionic acid + H2O
-
 Pseudomonas sp. 113 (R)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.10 additional information the enzyme has a single common active site for both reactions on L- and D-enantiomers, the reaction mechanismm does not proceed via an ester intermediate and not via a nucleophilic aspartate attacking the C-atom of the substrate to displace the halo-atom on contrast to the (S)-2-haloacid dehalogenase, EC 3.8.1.2. In the (S,R)-2-haloacid dehalogenase, a water molecule directly atacks the substrate for halide displacement, structure-function relationship, overview Pseudomonas sp. ?
-
 ?
3.8.1.10 additional information the enzyme has a single common active site for both reactions on L- and D-enantiomers, the reaction mechanismm does not proceed via an ester intermediate and not via a nucleophilic aspartate attacking the C-atom of the substrate to displace the halo-atom on contrast to the (S)-2-haloacid dehalogenase, EC 3.8.1.2. In the (S,R)-2-haloacid dehalogenase, a water molecule directly atacks the substrate for halide displacement, structure-function relationship, overview Pseudomonas sp. 113 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.8.1.2 More docking and structure analysis of enzyme mutants K151A and D180A in complex with substrate (S)-2-chloropropionic acid, molecular dynamics, overview Pseudomonas sp.
3.8.1.10 More structure comparisons, overview Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.8.1.2 L-2-haloacid dehalogenase
-
 Pseudomonas sp.
3.8.1.2 L-DEX YL
-
 Pseudomonas sp.
3.8.1.3 FAc-Dex FA1
-
 Burkholderia sp.
3.8.1.3 FAc-Dex H1
-
 Delftia acidovorans
3.8.1.3 fluoroacetate dehalogenase
-
 Delftia acidovorans
3.8.1.3 fluoroacetate dehalogenase
-
 Burkholderia sp.
3.8.1.10 DL-2-haloacid dehalogenase
-
 Pseudomonas sp.
3.8.1.10 DL-DEX 113
-
 Pseudomonas sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.8.1.2 additional information
-
 additional information single turnover Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.103 NADPH no activity with NADH Burkholderia sp.

General Information

EC Number General Information Comment Organism
3.8.1.2 evolution the enzyme belongs to the HAD superfamily Pseudomonas sp.
3.8.1.3 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.