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Information on EC 3.8.1.2 - (S)-2-haloacid dehalogenase and Organism(s) Pseudomonas putida and UniProt Accession Q52087
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3.8.1.2 (S)-2-haloacid dehalogenaseIUBMB 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)]
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Word Map
- 3.8.1.2
-
dehalogenation
- synthesis
-
haloacids
- l-2-haloacids
-
bioremediation
- l-2-chloropropionate
-
2-chloropropionic
- halide
- hymeniacidon
-
monochloroacetic
-
xanthobacter
-
dechlorination
- autotrophicus
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monobromoacetic
- chloroacetate
- haloalkane
- analysis
- environmental protection
The taxonomic range for the selected organisms is: Pseudomonas putida
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2-haloacid dehalogenase, l-haloacid dehalogenase, ph1421, deh99, l-2-dhlb, (s)-2-haloacid dehalogenase, dehalogenase iva, hadl aj1, l-had, 2-halocarboxylic acid dehalogenase ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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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dehalogenase IVa
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DL-2-haloacid dehalogenase [ambiguous]
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L-2-haloacid dehalogenase
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L-DEX
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L-DEX YL
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L-DEXs
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-halide hydrolysis
C-halide hydrolysis
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
(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)]
CAS REGISTRY NUMBER
COMMENTARY
37289-39-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-chloropropionate + H2O
(R)-2-hydroxypropionic acid + chloride
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-
-
?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
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-
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?
(R,S)-2-chloropropionic acid + H2O
(S)-lactic acid + (S)-2-chloropropionic acid + HCl
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?
DL-2-haloalkanoic acid + H2O
L-2-hydroxyalkanoic acid + D-2-hydroxyalkanoic acid + 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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?
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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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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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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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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
40°C: about 40% of maximal activity, 60°C: about 70% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25687
1 * 26000, SDS-PAGE, 1 * 25687, calculated from amino acid sequence
26000
1 * 26000, SDS-PAGE, 1 * 25687, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
1 * 26000, SDS-PAGE, 1 * 25687, calculated from amino acid sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and Pseudomonas putida hosts by using broad-host-range vectors
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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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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)
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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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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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
-
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
-
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
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
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
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