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Information on EC 3.8.1.10 - 2-haloacid dehalogenase (configuration-inverting)
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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
-
dehalogenation
-
l-2-haloalkanoic
- l-2-chloropropionate
- monochloroacetate
-
alpha-carbon
-
2-haloacids
-
decongestive
- xanthobacter
- autotrophicus
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
2-HAD, 2-haloalkanoic acid dehalogenase, 2-haloalkanoid acid halidohydrolase, DL DEX 113, DL-2-haloacid dehalogenase, DL-2-haloacid dehalogenase (inversion of configuration), DL-2-haloacid halidohydrolase (inversion of configuration), DL-DEX, DL-DEX 113, DL-DEX Mb, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DL-2-haloacid dehalogenase
DL-DEX 113
L-2-haloacid dehalogenase
L-DEX
L-DEX YL
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide
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)
-
-
(R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide
group I enzymes, including DL-2-haloacid dehalogenase and D-2-haloacid dehalogenase, catalyze the reaction without forming an ester intermediate. Instead, a solvent water molecule directly attacks the alpha-carbon atom of the substrate to release the halide ion. DL-2-haloacid dehalogenase acts on both enantiomers of the substrate
(S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide
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)
-
-
(S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide
group I enzymes, including DL-2-haloacid dehalogenase and D-2-haloacid dehalogenase, catalyze the reaction without forming an ester intermediate. Instead, a solvent water molecule directly attacks the alpha-carbon atom of the substrate to release the halide ion. DL-2-haloacid dehalogenase acts on both enantiomers of the substrate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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)]
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CAS REGISTRY NUMBER
COMMENTARY
89511-96-6
-
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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
(R)-2-chloropropionate + H2O
(S)-2-hydroxypropionate + chloride
-
-
-
?
(S)-2-chloropropionate + H2O
(R)-2-hydroxypropionate + chloride
-
-
-
?
2-bromo-2-methylpropionate + H2O
2-hydroxy-2-methylpropionate + bromide
slow substrate for the wild-type enzyme, but inhibitory for enzyme mutant D194N
-
-
?
tribromoacetic acid + H2O
carbon monoxide + carbon dioxide + HBr
-
-
-
?
(R)-2-chloropropionic acid + H2O
(S)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(R)-2-chloropropionic acid + H2O
(S)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(R)-2-chloropropionic acid + H2O
(S)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(R)-2-haloacid + H2O
(S)-2-hydroxyacid + halide
-
-
-
-
?
(R)-2-haloacid + H2O
(S)-2-hydroxyacid + halide
-
-
-
-
?
(R)-2-haloacid + H2O
(S)-2-hydroxyacid + halide
-
-
-
-
?
(R)-2-haloacid + H2O
(S)-2-hydroxyacid + halide
-
enzyme of 2-chloroacrylate grown cells
-
-
?
(R)-2-haloacid + H2O
(S)-2-hydroxyacid + halide
-
-
-
-
?
(R)-2-haloacid + H2O
(S)-2-hydroxyacid + halide
-
enzyme of 2-chloroacrylate grown cells
-
-
?
(S)-2-chloropropionic acid + H2O
(R)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(S)-2-chloropropionic acid + H2O
(R)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(S)-2-chloropropionic acid + H2O
(R)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
-
-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
-
-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
-
-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
-
enzyme of 2-chloroacrylate grown cells
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
-
-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
-
enzyme of 2-chloroacrylate grown cells
-
-
?
2-chlorobutyrate + H2O
2-hydroxybutyrate + chloride
-
-
-
?
2-chlorobutyrate + H2O
2-hydroxybutyrate + chloride
-
-
-
?
D-2-bromopropionate + H2O
L-lactate + bromide
-
-
-
?
D-2-chloropropionate + H2O
L-lactate + chloride
-
-
-
?
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
-
-
?
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
-
-
?
D-2-monochloropropionate + H2O
L-lactate + HCl
-
-
-
-
?
DL-2-chloropropionate + H2O
DL-lactate + HCl
-
-
-
-
?
L-2-monochloropropionate + H2O
D-lactate + HCl
-
-
-
-
?
additional information
?
-
DL-2-haloacid dehalogenase, DL-DEX, converts both enantiomers of the substrate
-
-
?
additional information
?
-
-
not: chloroacetamide, chloroacetaldehyde, 3-chloropropionate, best substrate: 2-halopropionate, followed by monohaloacetate, 2-halobutyrate, and 2-halovalerate in that order
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
not: chloroacetamide, chloroacetaldehyde, 3-chloropropionate, best substrate: 2-halopropionate, followed by monohaloacetate, 2-halobutyrate, and 2-halovalerate in that order
-
-
?
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
-
-
?
additional information
?
-
2-haloacid dehalogenases catalyse the hydrolytic dehalogenation of 2-haloalkanoic acids, cleaving the carbon-halide bond at the Calpha-atom position and releasing a halogen atom
-
-
?
additional information
?
-
-
2-haloacid dehalogenases catalyse the hydrolytic dehalogenation of 2-haloalkanoic acids, cleaving the carbon-halide bond at the Calpha-atom position and releasing a halogen atom
-
-
?
additional information
?
-
enzyme ps-2-HAD reveals its capacity to catalyse the dehalogenation of both L- and D-substrates
-
-
?
additional information
?
-
-
enzyme ps-2-HAD reveals its capacity to catalyse the dehalogenation of both L- and D-substrates
-
-
?
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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-chloropropionic acid + H2O
(S)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(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
-
-
-
-
?
(S)-2-chloropropionic acid + H2O
(R)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(S)-2-chloropropionic acid + H2O
(R)-2-hydroxypropionic acid + chloride
-
-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
-
-
-
-
?
additional information
?
-
DL-2-haloacid dehalogenase, DL-DEX, converts both enantiomers of the substrate
-
-
?
additional information
?
-
2-haloacid dehalogenases catalyse the hydrolytic dehalogenation of 2-haloalkanoic acids, cleaving the carbon-halide bond at the Calpha-atom position and releasing a halogen atom
-
-
?
additional information
?
-
-
2-haloacid dehalogenases catalyse the hydrolytic dehalogenation of 2-haloalkanoic acids, cleaving the carbon-halide bond at the Calpha-atom position and releasing a halogen atom
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-bromo-2-methylpropionate
an inhibitor of the D194N mutant enzyme and slow substrate of the wild-type enzyme
additional information
-
not: 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, Woodward reagent K
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
A Prospective Study of L-Dex Values in Breast Cancer Patients Pretreatment and Through 12 Months Postoperatively.
Breast Neoplasms
L-dex ratio in detecting breast cancer-related lymphedema: reliability, sensitivity, and specificity.
Breast Neoplasms
L-Dex, arm volume, and symptom trajectories 24 months after breast cancer surgery.
Breast Neoplasms
The Impact of L-Dex(®) Measurements in Assessing Breast Cancer-Related Lymphedema as Part of Routine Clinical Practice.
Lung Injury
Prophylaxis against lipopolysaccharide-induced lung injuries by liposome-entrapped dexamethasone in rats.
Lymphedema
A Prospective Study of L-Dex Values in Breast Cancer Patients Pretreatment and Through 12 Months Postoperatively.
Lymphedema
A Prospective Validation Study of Bioimpedance with Volume Displacement in Early-Stage Breast Cancer Patients at Risk for Lymphedema.
Lymphedema
Bioimpedance spectroscopy is not associated with a clinical diagnosis of breast cancer-related lymphedema.
Lymphedema
Correlation of Bioimpedance Spectroscopy with Risk Factors for the Development of Breast Cancer-Related Lymphedema.
Lymphedema
Correlation of L-Dex Bioimpedance Spectroscopy with Limb Volume and Lymphatic Function in Lymphedema.
Lymphedema
Does Lymphedema Severity Affect Quality of Life? Simple Question. Challenging Answers.
Lymphedema
EFFECTS OF COMPRESSION ON LYMPHEDEMA DURING RESISTANCE EXERCISE IN WOMEN WITH BREAST CANCER-RELATED LYMPHEDEMA: A RANDOMIZED, CROSS-OVER TRIAL.
Lymphedema
Heavy-load resistance exercise during chemotherapy in physically inactive breast cancer survivors at risk for lymphedema: a randomized trial.
Lymphedema
L-dex ratio in detecting breast cancer-related lymphedema: reliability, sensitivity, and specificity.
Lymphedema
L-Dex, arm volume, and symptom trajectories 24 months after breast cancer surgery.
Lymphedema
Patterns of Obesity and Lymph Fluid Level during the First Year of Breast Cancer Treatment: A Prospective Study.
Lymphedema
The Impact of L-Dex(®) Measurements in Assessing Breast Cancer-Related Lymphedema as Part of Routine Clinical Practice.
Lymphedema
The Role of Elastography in Diagnosis and Staging of Breast Cancer-Related Lymphedema.
Lymphedema
The use of bioimpedance spectroscopy to monitor therapeutic intervention in patients treated for breast cancer related lymphedema.
Lymphedema
Variation in Measurement Results Using Bioimpedance Spectroscopy to Determine Extracellular Fluid of Upper Extremity.
Obesity
Patterns of Obesity and Lymph Fluid Level during the First Year of Breast Cancer Treatment: A Prospective Study.
Pneumonia
Prophylaxis against lipopolysaccharide-induced lung injuries by liposome-entrapped dexamethasone in rats.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5 - 12
pH 9.5: about 50% of maximal activity, pH 12.0: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
additional information
evolution
Based on their substrate specificities and the configurations of their products, 2-HADs are classified into three types. DL-2-HADs catalyse the dehalogenation of both D- and L-2-haloalkanoic acids, inverting the stereochemistry at the Calpha-atom position and producing the corresponding L- and D-products, respectively. D- and L-2-HADs act specifically on only one enantiomer and cause inversion of Calpha-atom stereochemistry in the hydroxyalkanoic acid product. Enzymatic activity analysis of Pseudomonas syringae 2-HAD reveals its capacity to catalyse the dehalogenation of both L- and D-substrates, but the structure of ps-2-HAD is completely different from that of DehI, which is the only DL-2-HAD enzyme that is structurally characterized, bps-2-HAD shows similar overall folding to L-HADs. Thus ps-2-HAD has a distinct active site and a unique catalytic behaviour compared with other HADs
evolution
the reaction proceeds in two steps, in the first step, a catalytic aspartate residue nucleophilically attacks the alpha-carbon atom of the substrate to release the halide ion, resulting in the formation of an ester intermediate in which the aspartate residue is covalently bound to the alpha-carbon atom of the substrate. In the second step, the ester intermediate is hydrolyzed by a solvent water molecule. This mechanism is not restricted to this group of enzymes, e.g., fluoroacetate dehalogenase catalyzes the reaction in the same manner, although this enzyme is not evolutionarily related to the group II enzymes. Group I enzymes, including DL-2-haloacid dehalogenase and D-2-haloacid dehalogenase, catalyze the reaction without forming an ester intermediate. Instead, a solvent water molecule directly attacks the alpha-carbon atom of the substrate to release the halide ion. DL-2-haloacid dehalogenase is an extraordinary enzyme that acts on both enantiomers of the substrate
additional information
either the magnesium-binding cavity at least partially overlaps with the active site of ps-2-HAD or the coordinated residues or water molecules are involved directly in the catalytic reaction
additional information
-
either the magnesium-binding cavity at least partially overlaps with the active site of ps-2-HAD or the coordinated residues or water molecules are involved directly in the catalytic reaction
additional information
modeling of binding pocket and the active site and QM/QM calculations, docking study using (R)- and (S)-2-chloropropionates, overview. The binding site cavity is shielded from the solvent region, and is composed of eight hydrophobic residues (Trp37, Ala39, Phe40, Gly41, Ala192, Phe273, Ile274, and Ile277), and five hydrophilic residues (Asn117, Tyr120, Ser193, Asp194, and Tyr270)
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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). HDDL_ALCXX
296
0
32785
Swiss-Prot
-
Q88B12_PSESM
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
230
0
25545
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
68000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant native and selenomethionine-labeled wild-type enzyme and recombinant D194N enzyme mutant complexed with inhibitor 2-bromo-2-methylpropionate, 15 mg/mL protein in 10 mM Hepes-NaOH, pH 7.5, is mixed with 3 M sodium formate, 5% glycerol v/v, as the reservoir solution, X-ray diffraction structure determination and analysis at 1.7-2.7 A resolution
purified enzyme, sitting drop vapour diffusion method, mixing of equal volumes of 9 mg/ml protein in 50 mM Tris, pH 8.0, and 25 mM NaCl, and of reservoir solution consisting of 0.2 M MgCl2 hexahydrate, 20-26% PEG 4000, 0.1 M Tris, pH 8.5, and equilibration against 0.1 ml of reservoir solution, 4°C, overnight, soaking of crystals in KI, X-ray diffraction structure determination and analysis at 1.98-2.0 A resolution, single-wavelength anomalous dispersion method, modeling
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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
-
the mutant is almost inactive, the mutation destabilizes substrate orientation and affects the balance of the charge around the active site
D180A
-
the mutation destabilizes the rotation of the nucleophile D10, fixes catalytic water around D10, and prevents K151 from approaching D10
K151A
-
the mutant is almost inactive, the mutation destabilizes substrate orientation and affects the balance of the charge around the active site
D10A
site-directed mutagenesis, the D10A mutant shows over 50% reduced enzyme activity compared to the wild-type enzyme
D11A
site-directed mutagenesis, the D11A mutant shows highly reduced enzyme activity compared to the wild-type enzyme
D180A
site-directed mutagenesis, the D180A mutant shows over 50% reduced enzyme activity compared to the wild-type enzyme
D184A
site-directed mutagenesis, the mutant cannot be expressed recombinantly
D185A
site-directed mutagenesis, the mutant cannot be expressed recombinantly
D8A
site-directed mutagenesis, the D8A mutant retains about half the enzyme activity of the wild-type
K155A
site-directed mutagenesis, the mutant cannot be expressed recombinantly
T127A
site-directed mutagenesis, the mutant cannot be expressed recombinantly
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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dehalogenase activity of the cell-free extracts obtained from AW-1T cells grown in the presence of chlorate is up to 3.5fold higher than the cell-free extracts obtained from AW-1T cells grown in the presence of oxygen
high constitutive expression of the L-DEX gene. The expression of the L-DEX gene is relatively stable, and the highest upregulation (about 22fold) is observed in the cultures amended with L-2-chloropropionate after 18 h, which then decreases
dehalogenase activity of the cell-free extracts obtained from AW-1T cells grown in the presence of chlorate is up to 3.5fold higher than the cell-free extracts obtained from AW-1T cells grown in the presence of oxygen
dehalogenase activity of the cell-free extracts obtained from AW-1T cells grown in the presence of chlorate is up to 3.5fold higher than the cell-free extracts obtained from AW-1T cells grown in the presence of oxygen
-
high constitutive expression of the L-DEX gene. The expression of the L-DEX gene is relatively stable, and the highest upregulation (about 22fold) is observed in the cultures amended with L-2-chloropropionate after 18 h, which then decreases
high constitutive expression of the L-DEX gene. The expression of the L-DEX gene is relatively stable, and the highest upregulation (about 22fold) is observed in the cultures amended with L-2-chloropropionate after 18 h, which then decreases
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the enzyme is of interest for their potential use in bioremediation and in the synthesis of industrial chemicals
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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
brenda
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
brenda
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 sp., Pseudomonas putida, Pseudomonas sp. 113
brenda
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.
brenda
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., Pseudomonas sp. YL
brenda
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
brenda
Leigh, J.A.; Skinner, A.J.; Cooper, R.A.
Partial purification, stereospecificity and stoichiometry of three dehalogenases from a Rhizobium species
FEMS Microbiol. Lett.
49
353-356
1988
Rhizobium sp.
-
brenda
Weightman, A.J.; Weightman, A.L.; Slater, J.H.
Stereospecificity of 2-monochloropropionate dehalogenation by the two dehalogenases of Pseudomonas P3: evidence for two different dehalogenation mechanisms
J. Gen. Microbiol.
128
1755-1762
1982
Pseudomonas putida, Pseudomonas putida PP3
brenda
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 sp., Pseudomonas putida, Rhizobium sp., Pseudomonas sp. 113, Pseudomonas putida PP3
-
brenda
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
-
brenda
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
Pseudomonas putida, Pseudomonas sp. (O06652), Pseudomonas sp., Achromobacter xylosoxidans (Q59168), Pseudomonas sp. 113 (O06652), Pseudomonas putida AJ1
brenda
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, Pseudomonas sp., Pseudomonas sp. 113, Burkholderia cepacia KY
-
brenda
Brokamp, A.; Happe, B.; Schmidt, F.R.J.
Cloning and nucleotide sequence of a D,L-haloalkanoic acid dehalogenase encoding gene from Alcaligenes xylosoxidans ssp. denitrificans ABIV
Biodegradation
7
383-396
1997
Achromobacter xylosoxidans
brenda
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., Pseudomonas sp. YL
-
brenda
Kurihara, T.; Esaki, N.
Bacterial hydrolytic dehalogenases and related enzymes: occurrences, reaction mechanisms, and applications
Chem. Rec.
8
67-74
2008
Pseudomonas putida, Methylobacterium sp. CPA1 (A6BM74), Pseudomonas sp. (O06652), Pseudomonas sp. 113 (O06652), Pseudomonas putida PP3
brenda
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., Pseudomonas sp. YL
brenda
Kurihara, T.
A mechanistic analysis of enzymatic degradation of organohalogen compounds
Biosci. Biotechnol. Biochem.
75
189-198
2011
Pseudomonas sp., Pseudomonas sp. 113
brenda
Hou, Z.; Zhang, H.; Li, M.; Chang, W.
Structure of 2-haloacid dehalogenase from Pseudomonas syringae pv. tomato DC3000
Acta Crystallogr. Sect. D
69
1108-1114
2013
Pseudomonas syringae (Q88B12), Pseudomonas syringae
brenda
Siwek, A.; Omi, R.; Hirotsu, K.; Jitsumori, K.; Esaki, N.; Kurihara, T.; Paneth, P.
Binding modes of DL-2-haloacid dehalogenase revealed by crystallography, modeling and isotope effects studies
Arch. Biochem. Biophys.
540
26-32
2013
Methylobacterium sp. (A6BM74)
brenda
Peng, P.; Zheng, Y.; Koehorst, J.J.; Schaap, P.J.; Stams, A.J.M.; Smidt, H.; Atashgahi, S.
Concurrent haloalkanoate degradation and chlorate reduction by Pseudomonas chloritidismutans AW-1T
Appl. Environ. Microbiol.
83
e00325-17
2017
Pseudomonas chloritidismutans (V4PWY9), Pseudomonas chloritidismutans AW-1T (V4PWY9)
brenda
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