Information on EC 3.8.1.2 - (S)-2-haloacid dehalogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
3.8.1.2
-
RECOMMENDED NAME
GeneOntology No.
(S)-2-haloacid dehalogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-halide hydrolysis
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-chloroacrylate degradation I
-
-
Chloroalkane and chloroalkene degradation
-
-
Chlorocyclohexane and chlorobenzene degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
non-pathway related
-
-
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 hide
37289-39-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain RS5, cryptic gene
-
-
Manually annotated by BRENDA team
strain RS5, cryptic gene
-
-
Manually annotated by BRENDA team
Azotobacter sp.
strain RC26
-
-
Manually annotated by BRENDA team
Azotobacter sp. RC26
strain RC26
-
-
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
isolated from the Arctic marine environment
-
-
Manually annotated by BRENDA team
isolated from the Arctic marine environment
-
-
Manually annotated by BRENDA team
Pseudomonas putida No. 109
No. 109
-
-
Manually annotated by BRENDA team
YL
-
-
Manually annotated by BRENDA team
strain 113
-
-
Manually annotated by BRENDA team
strain CBS3 stain CBS3 <31,41>
-
-
Manually annotated by BRENDA team
isolated from the intertidal marine sponge Hymeniacidon perlevis
-
-
Manually annotated by BRENDA team
isolated from the intertidal marine sponge Hymeniacidon perlevis
-
-
Manually annotated by BRENDA team
strain OT3
-
-
Manually annotated by BRENDA team
strain OT3
-
-
Manually annotated by BRENDA team
gene DehRhb
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
-
DEH99 is a (S)-2-haloacid dehalogenase, which can degrade (S)-2-chloropropionic acid, (S)-2-bromopropionic acid, and iodoacetic acid
additional information
folding of the DehRhb monomer and active site structure with catalytic residue Asp18, overall structure modeling. The halogen cradle in enzyme DehRhb is formed by the side chains of Phe47, Ile51, Phe66, Asn125 and Trp185
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R,S)-2-bromopropionic acid + H2O
(S)-lactic acid + (S)-2-bromopropionic acid + HCl
show the reaction diagram
-
-
-
-
?
(R,S)-2-chloropropionic acid + H2O
(S)-lactic acid + (S)-2-chloropropionic acid + HCl
show the reaction diagram
(S)-2-bromopropionic acid + H2O
(R)-2-hydroxypropionate + bromide
show the reaction diagram
-
-
-
?
(S)-2-bromopropionic acid + H2O
(R)-2-hydroxypropionic acid + bromide
show the reaction diagram
(S)-2-chlorobutyric acid + H2O
(R)-2-hydroxybutyric acid + chloride
show the reaction diagram
(S)-2-chloropropionic acid + H2O
(R)-2-hydroxypropionate + chloride
show the reaction diagram
-
-
-
?
(S)-2-chloropropionic acid + H2O
(R)-2-hydroxypropionic acid + chloride
show the reaction diagram
(S)-2-chloropropionic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
show the reaction diagram
1,2-dichloroethane + H2O
?
show the reaction diagram
2,2-dichloropropionate + H2O
propionate + HCl
show the reaction diagram
-
-
-
-
?
2,2-dichloropropionic acid + H2O
?
show the reaction diagram
-
-
-
-
?
2,2-dichloropropionic acid + H2O
propionate + HCl
show the reaction diagram
-
-
-
-
?
2,3-dibromopropionate + H2O
?
show the reaction diagram
2,3-dichloropropionate + H2O
?
show the reaction diagram
2,3-dichloropropionic acid + H2O
3-chlorlactic acid + HCl
show the reaction diagram
2-bromoacetic acid + H2O
2-hydroxyacetate + bromide
show the reaction diagram
-
-
-
?
2-bromohexadecanoate + H2O
D-2-hydroxyhexadecanoate + HBr
show the reaction diagram
-
-
-
-
?
2-bromopropionic acid + H2O
?
show the reaction diagram
2-chloro-3-hydroxypropionate + H2O
glycerate + HCl
show the reaction diagram
2-chloro-n-butyrate + H2O
2-hydroxybutyrate + HCl
show the reaction diagram
2-chloroacetic acid + H2O
2-hydroxyacetate + chloride
show the reaction diagram
-
-
-
?
2-chloroacrylate + H2O
2-hydroxyacrylate + HCl
show the reaction diagram
-
-
-
-
?
2-chloropropionate + H2O
2-hydroxypropionate + chloride
show the reaction diagram
2-chloropropionate + H2O
lactate + HCl
show the reaction diagram
2-chloropropionic acid + H2O
?
show the reaction diagram
2-monobromobutyrate + H2O
?
show the reaction diagram
-
-
-
?
2-monochlorobutyrate + H2O
?
show the reaction diagram
alpha-bromophenylacetic acid + H2O
?
show the reaction diagram
-
-
-
-
?
dichloroacetate + H2O
?
show the reaction diagram
dichloroacetic acid + H2O
?
show the reaction diagram
DL-2-bromo-n-butyrate + H2O
?
show the reaction diagram
DL-2-bromobutyrate + H2O
?
show the reaction diagram
DL-2-bromopropionate + H2O
?
show the reaction diagram
-
-
-
-
?
DL-2-bromopropionic acid + H2O
?
show the reaction diagram
-
-
-
-
?
DL-2-chlorobutyrate + H2O
?
show the reaction diagram
-
-
-
-
?
DL-2-chloropropionate + H2O
?
show the reaction diagram
DL-2-haloalkanoic acid + H2O
L-2-hydroxyalkanoic acid + D-2-hydroxyalkanoic acid + halide
show the reaction diagram
fatty acids + H2O
?
show the reaction diagram
iodoacetic acid + H2O
acetic acid + iodide + H+
show the reaction diagram
L-2-bromobutanoate + H2O
2-hydroxybutanoate + HBr
show the reaction diagram
L-2-bromohexanoate + H2O
2-hydroxyhexanoate + HBr
show the reaction diagram
L-2-bromopropionate + H2O
lactate + HBr
show the reaction diagram
L-2-chloropropionate + H2O
?
show the reaction diagram
-
-
-
-
?
L-2-chloropropionate + H2O
D-2-hydroxypropionate + chloride
show the reaction diagram
-
-
-
-
?
L-2-chloropropionate + H2O
D-lactate + HCl
show the reaction diagram
L-2-chloropropionate + H2O
lactate + HCl
show the reaction diagram
L-2-chloropropionic acid + H2O
D-2-chloropropionic acid + H2O
show the reaction diagram
L-2-chloropropionic acid + H2O
D-2-hydroxypropionate + HCl
show the reaction diagram
-
-
-
-
?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
show the reaction diagram
monobromoacetate + H2O
glycolate + HBr
show the reaction diagram
monobromoacetate + H2O
hydroxyacetate + bromide
show the reaction diagram
-
-
-
-
?
monobromoacetic acid + H2O
acetic acid + bromide
show the reaction diagram
monochloroacetate + H2O
glycolate + HCl
show the reaction diagram
monochloroacetate + H2O
hydroxyacetate + chloride
show the reaction diagram
-
-
-
-
?
monoiodoacetate + H2O
glycolate + HI
show the reaction diagram
monoiodoacetate + H2O
hydroxyacetate + iodide
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-2-bromopropionic acid + H2O
(R)-2-hydroxypropionic acid + bromide
show the reaction diagram
-
-
-
-
?
(S)-2-chloropropionic acid + H2O
(R)-2-hydroxypropionic acid + chloride
show the reaction diagram
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
show the reaction diagram
M9P6K0
-
-
-
?
1,2-dichloroethane + H2O
?
show the reaction diagram
2,2-dichloropropionic acid + H2O
?
show the reaction diagram
-
-
-
-
?
2-chloropropionate + H2O
2-hydroxypropionate + chloride
show the reaction diagram
2-chloropropionate + H2O
lactate + HCl
show the reaction diagram
DL-2-haloalkanoic acid + H2O
L-2-hydroxyalkanoic acid + D-2-hydroxyalkanoic acid + halide
show the reaction diagram
iodoacetic acid + H2O
acetic acid + iodide + H+
show the reaction diagram
-
-
-
-
?
L-2-chloropropionic acid + H2O
D-2-chloropropionic acid + H2O
show the reaction diagram
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
show the reaction diagram
monobromoacetate + H2O
glycolate + HBr
show the reaction diagram
monochloroacetate + H2O
glycolate + HCl
show the reaction diagram
monoiodoacetate + H2O
glycolate + HI
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
dependent on
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
-
CuSO4
41% inhibition
iodoacetamide
-
-
mercury(II)-acetate
-
-
N-ethylmaleimide
-
-
p-Chloromercuriphenylsulfonic acid
-
-
p-mercuric chlorobenzoate
thiol reagents
Woodward reagent K
-
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2 - 4.9
(S)-2-chloropropionic acid
6.72
2-bromoacetic acid
recombinant enzyme, pH and temperature not specified in the publication
-
7.5
2-monochloropropionic acid
-
pH 8.5, 37C
1.3
Dichloroacetate
-
pH 9.4, 30C
1.7
L-2-bromobutanoate
pH 9.5, 70C
0.41
L-2-bromohexanoate
pH 9.5, 70C
2.1
L-2-bromopropionate
pH 9.5, 70C
0.37 - 19.5
L-2-chloropropionate
1.13
monobromoacetate
pH 7.9, 30C
0.15
monobromoacetic acid
-
pH 8.2, 25C
-
0.1 - 8
Monochloroacetate
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
47
L-2-chloropropionate
Pseudomonas sp.
-
comparison with mutant enzymes
additional information
additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.06
-
substrate (S)-2-chloropropionic acid, pH 7.3, 30C
0.7
Azotobacter sp.
-
coupled assay with lactate dehydrogenase
0.9
-
substrate: (S)-2-chloropropionic acid, pH 9.0, 22C, immobilized enzyme
3
-
substrate: (S)-2-chloropropionic acid, pH 9.0, 37C, immobilized enzyme
6.3
-
substrate: (S)-2-chloropropionic acid, pH 9.0, 50C, immobilized enzyme
20
-
substrate: (S)-2-chloropropionic acid, pH 9.0, 50C, soluble enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9
Azotobacter sp.
-
-
8.2
-
assay at
9 - 9.4
-
-
9.5
-
soluble and immobilized enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
the enzyme reaction is retarded below pH 6.0 and the reaction is spontaneously over pH 9.0
8 - 10
Azotobacter sp.
-
-
8 - 10.5
-
pH 8.0: about 50% of maximal activity, pH 10.5: about 80% of maximal activity
9 - 11.5
pH 9.0: about 45% of maximal activity, pH 11.5: about 70% of maximal activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 65
-
activity range, 20% of maximal activity at 10C, about 80% at 60C, inactivation above 65C
20 - 60
Azotobacter sp.
-
-
25 - 70
-
-
50 - 90
50C: about 40% of maximal activity, 90C: about 80% of maximal activity
additional information
-
enzyme covalently immobilized is stable between 30C and 85C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
the mutation from an acidic to a basic amino acid leads to an alteration in the enzyme pI valiue from 5.1 to 6.0
5.5
Azotobacter sp.
-
isoelectric focusing
6.2
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Polaromonas sp. (strain JS666 / ATCC BAA-500)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas sp. (strain YL)
Pseudomonas sp. (strain YL)
Pseudomonas sp. (strain YL)
Pseudomonas sp. (strain YL)
Ralstonia solanacearum (strain GMI1000)
Rhodococcus jostii (strain RHA1)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000 - 28000
25230
-
calculated from amino acid sequence
25400
-
calculated from amino acid sequence
25600
-
SDS-PAGE
25680
-
calculated from amino acid sequence
25900
-
calculated from amino acid sequence
26180
-
calculated from amino acid sequence
27430
-
calculated from amino acid sequence
31000
-
gel filtration
33600
-
calculated from amino acid sequence
34000
-
gel filtration
36000
-
gel filtration
38000
-
gel filtration
41000
-
gel filtration
49700
-
calculated apparent molecular weight
50000
-
gel filtration
58000
gel filtration
60000
-
gel filtration
64000
-
gel filtration
79000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; alpha/beta structure; mutant S175A
-
alpha/beta structure
-
crystal structures of enzyme complexed with monochloroacetate, L-2-chlorobutyrate, L-2-chloro-3-methylbutyrate, or L-2-chloro-4-methylvalerate are determined using the complex crystals prepared with the S175A mutant; mutant S175A
-
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
-
oil-microbatch method, in 200 mM NaCl and 20 mM Tris-HCl pH 8.0, 25.5% (w/v) polyethylene glycol 4000, 0.17 M ammonium acetate, 15% (w/v) glycerol and 85 mM sodium acetate buffer, pH 4.6, at 20C
-
refined to 1.9 A resolution. Crystal is an orderdisorder twin by reticular merohedry with a twin index of 10
-
apoenzyme and enzyme in intermediate state with substrate L-2-monochloropropionate and monochloroacetate
apoenzyme and enzyme in intermediate state with substrate L-2-monochloropropionate and monochloroacetate; three-dimensional structure of enzyme
-
three-dimensional structure of enzyme
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
the enzyme tolerates extreme pH conditions ranging from 4 to 10
723963
4.5 - 10.5
-
at 30C for 30 min
648277
6 - 11
-
-
648292
7.5 - 11
-
-
648301
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
recombinant enzyme DehRhb has a melting temperature of 67C, it is completely stable at 30C, loses 10% activity at 40 and 30% at 55C after 90mmin, 85% activity are remaining after 90 min at 50C, 14% activity remaining after 90 min at 60C
40
-
purified recombinant enzyme, 2 h, completely stable up to
50 - 90
the enzyme is stable to prolonged exposure to 50C, losing only 8% activity after 90 min incubation, as the temperature is increased the stability decreases, the enzyme is thermostable with a half-life of over 1 h at 70C
55
-
after 15 min loss of 50% activity
65
-
purified recombinant enzyme, 2 h, inactivation
70
4 h, enzyme remains fully active
80
4 h, 10% loss of activity
90
1 h, 70% loss of activity
additional information
Azotobacter sp.
-
activity and stability at different temperatures
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme retains approximately 30% of the overall activity after immobilization
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
acetonitrile
chloroform
dithiothreitol
Ethanol
Methanol
n-heptane
additional information
enzyme DehRhb has a relatively high tolerance to organic solvents, i.e. in ethanol, methanol, acetonitrile, or dimethylsulfoxide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, pH 7.5, 6 months
-
-20C, pH 7.5 + 50% glycerol, 6 months, strain YL
-
50 mM Tris sulfate, pH 7.5 + 0.01% NaN3 at 25C or -30C, 30 days with remaining 60% activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
HiPrep 26/10 column chromatography, Super Q Toyopearl 650M column chromatography, hydroxyapatite column chromatography, and Superdex 200 gel filtration
-
Ni-NTA column chromatography and gel filtration
recombinant N-terminally His- and S-tagged enzyme from Escherichia coli strain BMRosetta by affinity purification followed by gel filtration, to homogeneity
-
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3)-RIPL by nickel affinity chromatography and gel filtration
two-step method: heat treatment step that removes 90% of the impurities, followed by an acidification step that eliminates the remaining impurities. The easy purification procedure renders the production of this protein fast, cost effective, and suitable for large-scale production
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21-Codon Plus (DE3)-RIL cells
-
expressed in Escherichia coli in a tag-free form
expression in Escherichia coli
expression in Escherichia coli and Pseudomonas putida
-
expression in Escherichia coli and Pseudomonas putida hosts by using broad-host-range vectors
-
gene dehII, DNA and amino acid sequence determination and analysis
-
gene DehRhb, DNA and amino acid sequence determination and analysis, recombinant overexpression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)-RIPL
phylogenetic analysis
-
phylogenetic analysis, recombinant expression of N-terminally His- and S-tagged enzyme in Escherichia coli strain BMRosetta
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D11E
-
totally inactive in catalysis
D11N
-
totally inactive in catalysis
D11S
-
totally inactive in catalysis
D181N
-
totally inactive in catalysis
N178D
-
defective in catalysis
D11E
-
totally inactive in catalysis
-
D11N
-
totally inactive in catalysis
-
D11S
-
totally inactive in catalysis
-
D181N
-
totally inactive in catalysis
-
D180A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
K151A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
S118A
-
mutant with lower specific activity and higher KM-value
S175A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
D180A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
-
K151A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
-
S118A
-
mutant with lower specific activity and higher KM-value
-
S175A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
-
D180A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
-
K151A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
-
S118A
-
mutant with lower specific activity and higher KM-value
-
S175A
-
site-directed mutagenesis of a residue that strongly interacts with the substrate
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
the enzyme is covalently linked to an N-hydroxysuccinimidyl Sepharose resin to construct a highly specific sensor with long shelf life for the detection of L-2-haloacids
environmental protection
synthesis
additional information
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