Information on EC 3.8.1.3 - haloacetate dehalogenase

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

EC NUMBER
COMMENTARY hide
3.8.1.3
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RECOMMENDED NAME
GeneOntology No.
haloacetate dehalogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
haloacetate + H2O = glycolate + halide
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-halide hydrolysis
dehalogenation
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,2-dichloroethane degradation
-
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butachlor degradation
-
-
Chloroalkane and chloroalkene degradation
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-
Chlorocyclohexane and chlorobenzene degradation
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fluoroacetate degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
haloacetate halidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37289-40-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain B
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-
Manually annotated by BRENDA team
mouse
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-
Manually annotated by BRENDA team
strain OT3
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-
Manually annotated by BRENDA team
strain OT3
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Synergistetes bacterium
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-chloropropionate + H2O
2-hydroxypropionate + chloride
show the reaction diagram
3-chlorobutyrate + H2O
3-hydroxybutyrate + chloride
show the reaction diagram
3-chloropropionate + H2O
3-hydroxypropionate + chloride
show the reaction diagram
chloroacetate + H2O
acetate + chloride
show the reaction diagram
chloroacetate + H2O
glycolate + chloride
show the reaction diagram
fluoroacetate + H2O
glycolate + fluoride
show the reaction diagram
haloacetate + H2O
glycolate + halide
show the reaction diagram
monobromoacetate + H2O
glycolate + HBr
show the reaction diagram
monochloroacetate + H2O
glycolate + HCl
show the reaction diagram
monofluoroacetate + H2O
glycolate + HF
show the reaction diagram
monoiodoacetate + H2O
glycolate + HI
show the reaction diagram
tyrosine-phosphorylated proteins + H2O
protein + phosphate
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
2-chloropropionate + H2O
2-hydroxypropionate + chloride
show the reaction diagram
3-chlorobutyrate + H2O
3-hydroxybutyrate + chloride
show the reaction diagram
3-chloropropionate + H2O
3-hydroxypropionate + chloride
show the reaction diagram
chloroacetate + H2O
glycolate + chloride
show the reaction diagram
fluoroacetate + H2O
glycolate + fluoride
show the reaction diagram
haloacetate + H2O
glycolate + halide
show the reaction diagram
monobromoacetate + H2O
glycolate + HBr
show the reaction diagram
monochloroacetate + H2O
glycolate + HCl
show the reaction diagram
monofluoroacetate + H2O
glycolate + HF
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
1,2-epoxy-3-(p-nitrophenoxy)propane
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1-chloro-2,3-dinitrobenzene
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AgCl2
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Aromatic acids
-
-
-
chloride
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strain AD29
fatty acids
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-
HgCl2
iodoacetamide
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-
N-ethylmaleimide
p-chloromercuribenzoate
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p-Chloromercuriphenylsulfonate
thiol reagents
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
Chloroacetate
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-
3.8
fluoroacetate
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25°C
0.18 - 0.33
Monochloroacetate
0.7 - 2
monofluoroacetate
1.1
monoiodoacetate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.6
1,2-epoxy-3-(p-nitrophenoxy)propane
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-
5.61
1-chloro-2,3-dinitrobenzene
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
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H1 recombinant in Butyrivibrio fibrisolvens
38.4
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crystallized
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
recombinant in Butyrifibrio fibrisolvens
10
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
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-
7.5 - 10
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pH 7.5: about 30% of maximal activity, pH 10.0: about 80% of maximal activity
8 - 10
8 - 11
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-
8 - 10
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activity below 50% above pH 10 and below pH 7,5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 30
30 - 50
30 - 60
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-
30 - 50
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30 - 60
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
2 * 27000, H2, SDS-PAGE
33000
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2 * 33000, SDS-PAGE
33258
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2 * 33258, H1
41000
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mouse
42000
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gel filtration
43000
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gel filtration
67000
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gel filtration; H1 recombinant in E. coli
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the domain proximal to the active site which is responsible for important specific interaction of low molecular weight substrates with the enzymes of the haloacid dehalogenase superfamily is missing in MDP-1, comparison of domain structures within the enzyme family
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant D104A in compex with fluoroacetate, X-ray diffraction structure determination and analysis at 1.2 A resolution
microbatch crystallization, 2.0 A crystal structure
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
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210644, 210652
6 - 10
7 - 9.5
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli
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recombinant wild-type and mutant fusion proteins from Escherichia coli, the tags are removed
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Butyrivibrio fibrisolvens, H1
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expression in Escherichia coli BL21(DE3) of wild-type and mutant enzymes fused to the calmodulin binding peptide CBP from mouse or to CBP and FLAG from yeast
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expression in Escherichia coli, H1, H2
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expression in Escherichia coli, H1, H2; expression in Pseudomonas spp., H1, H2
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expression in yeast, H1
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expression of wild-type and mutant enzymes in Escherichia coli
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mutant expression in Escherichia coli, H1
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
haloacids monochloroacetate and monobromoacetate induces the haloacetate dehalogenase
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D104A
site-directed mutagenesis
W150F
site-directed mutagenesis
D104A
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site-directed mutagenesis
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W150F
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site-directed mutagenesis
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D105N
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site-directed mutagenesis, catalytic site mutant, shows reduced activity, but reactivation occurs due to hydrolytic deamination of the mutant Asn105 to the wild-type Asp105, reactivation in a time- and temperature-dependent manner
H272N
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mutant, no activity, substrate blocks binding pocket
D105N
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site-directed mutagenesis, catalytic site mutant, shows reduced activity, but reactivation occurs due to hydrolytic deamination of the mutant Asn105 to the wild-type Asp105, reactivation in a time- and temperature-dependent manner
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D10E
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site-directed mutagenesis, inactive catalytic site residue mutant
D10N
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site-directed mutagenesis, inactive catalytic site residue mutant
D121N
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site-directed mutagenesis, catalytic site residue mutant, 0.4% activity compared to the wild-type enzyme
D122N
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site-directed mutagenesis, catalytic site residue mutant, 0.1% activity compared to the wild-type enzyme
D12N
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site-directed mutagenesis, catalytic site residue mutant, 8% activity compared to the wild-type enzyme
K99R
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site-directed mutagenesis, catalytic site residue mutant, 1.4% activity compared to the wild-type enzyme
N126D
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site-directed mutagenesis, 52% activity compared to the wild-type enzyme
S68A
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site-directed mutagenesis, catalytic site residue mutant, 0.1% activity compared to the wild-type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
-
selection marker on cloning vectors
biotechnology
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