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EC Tree
IUBMB Comments Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2. [See also EC 3.8.1.9 (R)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
The taxonomic range for the selected organisms is: Pseudomonas putida The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2-haloacid dehalogenase, l-2-dhlb, l-haloacid dehalogenase, ph1421, deh99, (s)-2-haloacid dehalogenase, dehalogenase iva, hadl aj1, l-had, 2-halocarboxylic acid dehalogenase ii,
more
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2-halo acid dehalogenase
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2-haloacid dehalogenase[ambiguous]
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2-haloacid halidohydrolase[ambiguous]
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2-haloalkanoic acid dehalogenase
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2-haloalkanoid acid halidohydrolase
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2-halocarboxylic acid dehalogenase II
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DL-2-haloacid dehalogenase [ambiguous]
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L-2-haloacid dehalogenase
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(S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide
(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
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(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
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C-halide hydrolysis
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(S)-2-haloacid halidohydrolase
Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2. [See also EC 3.8.1.9 (R)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
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(S)-2-chloropropionate + H2O
(R)-2-hydroxypropionic acid + chloride
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?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
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?
2,3-dibromopropionate + H2O
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?
2,3-dichloropropionate + H2O
?
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?
2-monobromobutyrate + H2O
?
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?
2-monochlorobutyrate + H2O
?
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?
L-2-chloropropionate + H2O
D-lactate + HCl
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?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
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?
(R,S)-2-chloropropionic acid + H2O
(S)-lactic acid + (S)-2-chloropropionic acid + HCl
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?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
2,3-dibromopropionate + H2O
?
2,3-dichloropropionic acid + H2O
3-chlorlactic acid + HCl
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?
2-bromopropionic acid + H2O
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?
2-chloro-3-hydroxypropionate + H2O
glycerate + HCl
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?
2-chloro-n-butyrate + H2O
2-hydroxybutyrate + HCl
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?
2-chloropropionic acid + H2O
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alpha-bromophenylacetic acid + H2O
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DL-2-bromo-n-butyrate + H2O
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DL-2-bromopropionic acid + H2O
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?
DL-2-haloalkanoic acid + H2O
L-2-hydroxyalkanoic acid + D-2-hydroxyalkanoic acid + halide
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?
fatty acids + H2O
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monohaloacids, short chain length C2 to C4
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L-2-chloropropionate + H2O
D-lactate + HCl
L-2-chloropropionic acid + H2O
D-2-hydroxypropionic acid + HCl
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?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
monobromoacetate + H2O
glycolate + HBr
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?
monochloroacetate + H2O
glycolate + HCl
monoiodoacetate + H2O
glycolate + HI
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?
additional information
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(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
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(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
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(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
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?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
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reaction by inversion of the configuration in a mixture of dimethylsulfoxide and buffer, but in presence of stoichiometric amounts of water proceeds without inversion of the configuration contrary to the behavior in an aqueous environment
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2,3-dibromopropionate + H2O
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2,3-dibromopropionate + H2O
?
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L-2-chloropropionate + H2O
D-lactate + HCl
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?
L-2-chloropropionate + H2O
D-lactate + HCl
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L-2-chloropropionate + H2O
D-lactate + HCl
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L-2-chloropropionate + H2O
D-lactate + HCl
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L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
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L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
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L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
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monochloroacetate + H2O
glycolate + HCl
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monochloroacetate + H2O
glycolate + HCl
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additional information
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the alpha-helical structure of the enzyme plays a significant role during catalysis, while beta-sheet formation is a functional disadvantage. Analysis of environment-induced conformational and functional changes of 2-haloacid dehalogenase is informative for understanding the molecular basis of its stability and the design of the enzyme for future biotechnological applications in conjunction with its biochemical properties
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additional information
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the alpha-helical structure of the enzyme plays a significant role during catalysis, while beta-sheet formation is a functional disadvantage. Analysis of environment-induced conformational and functional changes of 2-haloacid dehalogenase is informative for understanding the molecular basis of its stability and the design of the enzyme for future biotechnological applications in conjunction with its biochemical properties
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L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
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?
DL-2-haloalkanoic acid + H2O
L-2-hydroxyalkanoic acid + D-2-hydroxyalkanoic acid + halide
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?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
monochloroacetate + H2O
glycolate + HCl
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?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
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L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
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L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
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Ag+
1 mM, no activity is retained
Ca2+
1 mM, induced 3.4% decrease in alpha-helix, 4.4% increase in beta-sheet, respectively, with less than 25% activity loss in activity
Cu2+
1 mM, induces the transition of alpha-helix to beta-sheet and random coil at the same time with more than half of the enzymatic activity loss
Hg2+
1 mM, no activity is retained
Zn2+
1 mM, induced 5.1% decrease in alpha-helix, 5.4% increase in beta-sheet, respectively, with less than 25% activity loss in activity
additional information
little effects on alpha-helix and HadL AJ1 activity are observed with the presence of 1 mM Co2+
additional information
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little effects on alpha-helix and HadL AJ1 activity are observed with the presence of 1 mM Co2+
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p-mercuric chlorobenzoate
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3.8
L-2-chloropropionate
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pH 10.5, 30°C
1
Monochloroacetate
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pH 10.5, 30°C
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additional information
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9 - 11
pH 9.0: about 60% of maximal activity, pH 11.0: about 60% of maximal activity
7 - 9
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the enzyme reaction is retarded below pH 6.0 and the reaction is spontaneously over pH 9.0
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40 - 60
40°C: about 40% of maximal activity, 60°C: about 70% of maximal activity
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SwissProt
brenda
AJ1
SwissProt
brenda
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brenda
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HADL_PSEPU
227
0
25687
Swiss-Prot
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25687
1 * 26000, SDS-PAGE, 1 * 25687, calculated from amino acid sequence
26000
1 * 26000, SDS-PAGE, 1 * 25687, calculated from amino acid sequence
25230
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calculated from amino acid sequence
33600
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calculated from amino acid sequence
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homodimer
2 * 26800, SDS-PAGE
tetramer
1 * 26000, SDS-PAGE, 1 * 25687, calculated from amino acid sequence
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D10N
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Asn10 of the mutant enzyme is spontaneously deaminated to yield Asp, though slowly, causing increasing activity of the mutant preparation
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7 - 8
24 h, structural and functional stability
757261
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55
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after 15 min loss of 50% activity
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DMSO
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the stereochemistry of the product obtained from racemic 2-bromopropionic acid by the action of celite-immobilized disrupted cells in dimethylsulfoxide differs from that of the enantiomer obtained in an aqueous buffer
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expression in Escherichia coli BL21
expression in Escherichia coli
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expression in Escherichia coli and Pseudomonas putida hosts by using broad-host-range vectors
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synthesis
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production of D-lactate in industry
synthesis
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production of optically active 2-hydroxyalkanoic acids and 2-haloalkanoic acids for chiral synthesis in industry
synthesis
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production of (S)-2-chloropropionic acid, which is used in the synthesis of optically active phenoxypropionic acid herbicides
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Motosugi, K; Esahi, N.; Soda, K.
Enzymatic preparation of D- and L-lactic acid from racemic 2-chloropropionic acid
Biotechnol. Bioeng.
26
805-806
1984
Pseudomonas putida, Pseudomonas sp., Pseudomonas sp. 113
brenda
Motosugi, K.; Esahi, N.; Soda, K.
Purification and properties of 2-halo acid dehalogenase
Agric. Biol. Chem.
46
837-838
1982
Pseudomonas putida
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brenda
Jones, D.H.A.; Barth, P.T.; Byrom, D.; Thomas, C.M.
Nucleotide sequence of the structural gene encoding a 2-haloalkanoic acid dehalogenase of Pseudomonas putida strain AJ1 and purification of the encoded protein
J. Gen. Microbiol.
138
675-683
1992
Pseudomonas putida, Pseudomonas putida (Q52087), Pseudomonas putida AJ1 (Q52087)
brenda
Onda, M; Motosugi, K.; Nakajima, H.
A new approach for enzymatic synthesis of D-3-chlorolactic acd from racemic 2,3-dichloropropionic acid by halo acid dehalogenase
Agric. Biol. Chem.
54
3031-3033
1990
Pseudomonas putida, Rhizobium sp., Pseudomonas putida No. 109
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brenda
Hasan, A.K.M.Q.; Motosugi, K.; Esaki, N.; Soda, K.
Total conversion of racemic 2-chloropropionic acid into D-lactate by combination of enzymic and chemical dehalogenations
J. Ferment. Bioeng.
72
481-482
1991
Pseudomonas putida
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brenda
Vyazmensky, M.; Geresh, S.
Substrate specificity and product stereochemistry in the dehalogenation of 2-haloacids with the crude enzyme preparation from Pseudomonas putida
Enzyme Microb. Technol.
22
323-328
1998
Xanthobacter autotrophicus, Pseudomonas putida, Pseudomonas putida No. 109
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brenda
Esaki, N.; Kurihara, T.; Li, Y.F.; Ichiyama, S.
Novel mechanism of enzymatic hydrolysis involving cyanoalanine intermediate revealed by mass spectrometric monitoring of an enzyme reaction
ICR Annual Report
7
46-47
2001
Pseudomonas putida, Pseudomonas putida YL
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brenda
Barth, P.T.; Bolton, L.; Thomson, J.C.
Cloning and partial sequencing of an operon encoding two Pseudomonas putida haloalkanoate dehalogenases of opposite stereospecificity
J. Bacteriol.
174
2612-2619
1992
Pseudomonas putida, Pseudomonas putida AJ1
brenda
Kawasaki, H.; Toyama, T.; Maeda, T.; Nishino, H.; Tonomura K.
Cloning and sequence analysis of a plasmid-encoded 2-haloacid dehalogenases gene from Pseudomonas putida No. 109
Biosci. Biotechnol. Biochem.
58
160-163
1994
Pseudomonas putida, Pseudomonas putida No. 109
brenda
Kurihara, T.; Liu, J.Q.; Nardi-Dei, V.; Koshikawa, H.; Esaki, N.; Soda, K.
Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino acid residues
J. Biochem.
117
1317-1322
1995
Burkholderia cepacia, Burkholderia cepacia MBA4, Moraxella sp., Moraxella sp. B, Pseudomonas putida, Pseudomonas putida AJ1, Pseudomonas putida No. 109, Pseudomonas sp., Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
brenda
Wang, Y.; Cao, X.; Feng, Y.; Xue, S.
Environment-induced conformational and functional changes of L-2-haloacid dehalogenase
J. Biosci. Bioeng.
121
491-496
2016
Pseudomonas putida (Q52087), Pseudomonas putida
brenda