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Information on EC 3.8.1.10 - 2-haloacid dehalogenase (configuration-inverting) and Organism(s) Pseudomonas sp. and UniProt Accession O06652
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3.8.1.10 2-haloacid dehalogenase (configuration-inverting)IUBMB Comments
Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (R)- and (S)-hydroxyalkanoic acids, respectively, with inversion of configuration at C-2. The enzyme from Pseudomonas sp. 113 acts on 2-haloalkanoic acids whose carbon chain lengths are five or less. [See also EC 3.8.1.2 (S)-2-haloacid dehalogenase, EC 3.8.1.9 (R)-2-haloacid dehalogenase and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
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Word Map
- 3.8.1.10
- lymphedema
-
bioimpedance
-
cancer-related
-
dehalogenation
-
l-2-haloalkanoic
-
2-haloacids
- l-2-chloropropionate
-
alpha-carbon
- monochloroacetate
-
decongestive
- autotrophicus
- xanthobacter
- synthesis
The taxonomic range for the selected organisms is: Pseudomonas sp.
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
l-dex, l-2-haloacid dehalogenase, dl-2-haloacid dehalogenase, dl-dex, 2-haloalkanoic acid dehalogenase, l-dex yl, ps-2-had, dl-dex 113, 2-had, dl-dex mb, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-haloalkanoic acid dehalogenase
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-
-
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2-haloalkanoid acid halidohydrolase
-
-
-
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DL DEX 113
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-
-
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DL-2-haloacid dehalogenase
DL-2-haloacid dehalogenase (inversion of configuration)
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-
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DL-2-haloacid halidohydrolase (inversion of configuration)
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-
-
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DL-DEXi
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-
-
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DL-2-haloacid dehalogenase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehalogenation
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-2-haloacid dehalogenase (configuration-inverting)
Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (R)- and (S)-hydroxyalkanoic acids, respectively, with inversion of configuration at C-2. The enzyme from Pseudomonas sp. 113 acts on 2-haloalkanoic acids whose carbon chain lengths are five or less. [See also EC 3.8.1.2 (S)-2-haloacid dehalogenase, EC 3.8.1.9 (R)-2-haloacid dehalogenase and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
CAS REGISTRY NUMBER
COMMENTARY
89511-96-6
-
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
(R)-2-chloropropionic acid + H2O
(S)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(S)-2-chloropropionic acid + H2O
(R)-2-hydroxypropionic acid + chloride
-
-
-
-
?
D-2-monochloropropionate + H2O
L-lactate + HCl
-
-
-
-
?
DL-2-chloropropionate + H2O
DL-lactate + HCl
-
-
-
-
?
L-2-monochloropropionate + H2O
D-lactate + HCl
-
-
-
-
?
D-2-chloropropionate + H2O
L-lactate + HCl
a step preceding the dehalogenation is partly rate-limiting when D-2-chloropropionate is used as the substrate
-
-
?
(R)-2-haloacid + H2O
(S)-2-hydroxyacid + halide
-
-
-
-
?
(R)-2-haloacid + H2O
(S)-2-hydroxyacid + halide
-
enzyme of 2-chloroacrylate grown cells
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
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-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
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enzyme of 2-chloroacrylate grown cells
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-
?
additional information
?
-
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not: chloroacetamide, chloroacetaldehyde, 3-chloropropionate, best substrate: 2-halopropionate, followed by monohaloacetate, 2-halobutyrate, and 2-halovalerate in that order
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-
?
additional information
?
-
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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
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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
(R)-2-chloropropionic acid + H2O
(S)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(R)-2-haloacid + H2O
(S)-2-hydroxyacid + halide
-
-
-
-
?
(S)-2-chloropropionic acid + H2O
(R)-2-hydroxypropionic acid + chloride
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-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not: 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, Woodward reagent K
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
68000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D180A
-
the mutation destabilizes the rotation of the nucleophile D10, fixes catalytic water around D10, and prevents K151 from approaching D10
K151A
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the mutant is almost inactive, the mutation destabilizes substrate orientation and affects the balance of the charge around the active site
additional information
additional information
each of the 26 residues with charged and polar side chains, which are conserved between enzyme and D-2-haloacid dehalogenase, is mutated, Thr65, Glu69 and Asp194 are found to be essential
additional information
-
each of the 26 residues with charged and polar side chains, which are conserved between enzyme and D-2-haloacid dehalogenase, is mutated, Thr65, Glu69 and Asp194 are found to be essential
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
15 min 50% loss of activity for D-2-chloropropionic acid and 40% loss of activity for L-2-chloropropionic acid
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM potassium phosphate buffer containing 50% glycerol, pH 7.5, 1 year
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, no significant sequence similarity between enzyme and L-2-haloacid dehalogenase is found, however, enzyme has significant sequence similarity with D-2-haloacid dehalogenase fom Pseudomonas putide AJ1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Motosugi, K; Esahi, N.; Soda, K.
Bacterial assimilation of D- and L-2-chloropropionates and occurrence of a new dehalogenase
Arch. Microbiol.
131
179-183
1982
Pseudomonas sp., Pseudomonas sp. 113
Motosugi, K; Esahi, N.; Soda, K.
Purification and properties of a new enzyme, DL-2-haloacid dehalogenase, from Pseudomonas sp.
J. Bacteriol.
150
522-527
1982
Pseudomonas sp., Pseudomonas sp. 113
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
Stringfellow, J.M.; Cairns, S.S.; Cornish, A.; Cooper, R.A.
Haloalkanoate dehalogease II (DehE) of a Rhizobium sp.molecular analysis of the gene and formation of carbon monoxide from trihaloacetate by the enzyme
Eur. J. Biochem.
250
789-793
1997
Pseudomonas sp., Rhizobium sp.
Liu, J.Q.; Kurihara, T.; Hasan, A.K.M.Q.; Nardi-Dei, V.; Koshikawa, H.; Esaki, N.; Soda, K.
Purification and characterization of thermostable and nonthermostable 2-haloacid dehalogenases with different stereospecificities from Pseudomonas sp. strain YL
Appl. Environ. Microbiol.
60
2389-2393
1994
Pseudomonas sp.
Nardi-Dei, V.; Kurihara, T.; Park, C.; Miyagi, M.; Tsunasawa, S.; Soda, K.; Esaki, N.
DL-2-Haloacid dehalogenase from Pseudomonas sp. 113 is a new class of dehalogenase catalyzing hydrolytic dehalogenation not involving enzyme-substrate ester intermediate
J. Biol. Chem.
274
20977-20981
1999
Pseudomonas sp., Pseudomonas sp. 113
Soda, K.; Kurihara, T.; Liu, J.Q.; Nardi-Dei, V.; Park, C.; Miyagi, M.; Tsunasawa, S.; Esaki, N.
Bacterial 2-haloacid dehalogenases: Structures and catalytic properties
Pure Appl. Chem.
68
2097-2103
1996
Pseudomonas putida, Pseudomonas putida PP3, Pseudomonas sp., Pseudomonas sp. 113, Rhizobium sp.
-
Kurihara, T.; Esaki, N.; Soda, K.
Bacterial 2-haloacid dehalogenases: structures and reaction mechanisms
J. Mol. Catal. B
10
57-65
2000
Pseudomonas sp., Pseudomonas sp. 113
-
Nardi-Dei, V.; Kurihara, T.; Park, C.; Esaki, N.; Soda, K.
Bacterial DL-2-haloacid dehalogenase from Pseudomonas sp. strain 113: gene cloning and structural comparison with D- and L-2-haloacid dehalogenases
J. Bacteriol.
179
4232-4238
1997
Achromobacter xylosoxidans (Q59168), Pseudomonas putida, Pseudomonas putida AJ1, Pseudomonas sp. (O06652), Pseudomonas sp., Pseudomonas sp. 113 (O06652)
Ohkouchi, Y.; Koshikawa, H.; Terashima, Y.
Cloning and expression of DL-2-haloacid dehalogenase gene from Burkholderia cepacia
Water Sci. Technol.
42
261-268
2000
Burkholderia cepacia, Burkholderia cepacia KY, Pseudomonas sp., Pseudomonas sp. 113
-
Hasan, A.K.M.Q.; Takada, H.; Koshikawa, H.; Liu, J.Q.; Kurihara, T.; Esaki, N.; Soda, K.
Two kinds of 2-halo acid dehalogeases fromm Pseudomonas sp. YL induced by 2-chloroacrylates and 2-chloropropionate
Biosci. Biotechnol. Biochem.
58
1599-1602
1994
Pseudomonas sp.
-
Kurihara, T.; Esaki, N.
Bacterial hydrolytic dehalogenases and related enzymes: occurrences, reaction mechanisms, and applications
Chem. Rec.
8
67-74
2008
Methylobacterium sp. CPA1 (A6BM74), Pseudomonas putida, Pseudomonas putida PP3, Pseudomonas sp. (O06652), Pseudomonas sp. 113 (O06652)
Nakamura, T.; Yamaguchi, A.; Kondo, H.; Watanabe, H.; Kurihara, T.; Esaki, N.; Hirono, S.; Tanaka, S.
Roles of K151 and D180 in L-2-haloacid dehalogenase from Pseudomonas sp. YL: Analysis by molecular dynamics and ab initio fragment molecular orbital calculations
J. Comput. Chem.
30
2625-2634
2009
Pseudomonas sp.
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