Information on EC 3.8.1.7 - 4-chlorobenzoyl-CoA dehalogenase

Word Map on EC 3.8.1.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.8.1.7
-
RECOMMENDED NAME
GeneOntology No.
4-chlorobenzoyl-CoA dehalogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-halide hydrolysis
dehalogenation
hydrolysis of C-halide
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-chlorobenzoate degradation
-
-
Fluorobenzoate degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
4-chlorobenzoyl CoA chlorohydrolase
Specific for dehalogenation at the 4-position. Can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position. This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
141583-18-8
-
141955-45-5
dehalogenase, 4-chlorobenzoyl coenzyme A (Pseudomonas strain CBS-3 clone pMMB22 reduced)
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 4-CB1
-
-
Manually annotated by BRENDA team
strain TM-1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
FcbB identified by metagenomic analysis (PCR)
-
-
Manually annotated by BRENDA team
a 2,4,5,6-tetrachloroisophthalonitrile (chlorothalonil)-degrading strain
UniProt
Manually annotated by BRENDA team
IEGM896, gene fcbB
-
-
Manually annotated by BRENDA team
IEGM896, gene fcbB
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4,5,6-tetrachloroisophthalonitrile + H2O
4-hydroxy-trichloroisophthalonitrile + chloride
show the reaction diagram
2,4-dichlorobenzoyl-CoA + H2O
?
show the reaction diagram
3,4-dichlorobenzoyl-CoA + H2O
?
show the reaction diagram
4-bromobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + bromide
show the reaction diagram
4-bromophenacyl-CoA + H2O
4-hydroxyphenacyl-CoA + bromide
show the reaction diagram
-
-
-
-
?
4-chloro-2-nitrobenzoyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
4-chloro-3-methylbenzoyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
4-chloro-3-nitrobenzoyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
4-chlorobenzoate + H2O
4-hydroxybenzoate + chloride
show the reaction diagram
4-chlorobenzoyl-3'-dephospho-CoA + H2O
4-hydroxybenzoyl-3'-dephospho-CoA + chloride
show the reaction diagram
-
-
-
-
?
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
show the reaction diagram
4-chlorobenzoyl-dithio-CoA + H2O
4-hydroxybenzoyl-dithio-CoA + chloride
show the reaction diagram
-
-
-
-
?
4-chlorobenzoyl-epsilon-CoA + H2O
4-hydroxybenzoyl-epsilon-CoA + chloride
show the reaction diagram
-
-
-
-
?
4-chlorobenzoyl-pantetheine + H2O
4-hydroxybenzoyl-pantetheine + chloride
show the reaction diagram
-
very low activity
-
-
?
4-chlorobenzoyl-pantetheine phosphate + H2O
4-hydroxybenzoyl-pantetheine phosphate + chloride
show the reaction diagram
-
-
-
-
?
4-fluorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + fluoride
show the reaction diagram
4-iodobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + 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
2,4,5,6-tetrachloroisophthalonitrile + H2O
4-hydroxy-trichloroisophthalonitrile + chloride
show the reaction diagram
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme A
-
-
additional information
Chd dehalogenates chlorothalonil under anaerobic and aerobic conditions and does not require the presence of cofactors such as CoA and ATP
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
activates
additional information
no activating effects by Cu2+, Ba2+, Mg2+, or Ni2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
complete inhibition, recovered by the subsequent supplementation with Zn2+
3'-AMP
-
weak inhibitor
3'-Dephospho-CoA
-
-
4-Chlorobenzoate
4-chlorobenzoyl-coenzyme A
-
competitive
4-hydroxybenzoyl-3'-dephospho-CoA
-
competitive
4-hydroxybenzoyl-CoA
-
competitive
4-hydroxybenzoyl-dithio-CoA
-
competitive
4-methylbenzoyl-3'-dephospho-CoA
-
competitive
4-methylbenzoyl-CoA
-
competitive
5'-ADP
-
weak inhibitor
5'-AMP
-
weak inhibitor
5,5'-dithiobis(2-nitrobenzoate)
-
-
adenosine
-
weak inhibitor
adenosine 3',5'-bisphosphate
-
weak inhibitor
Ag+
-
5 mM
ATP
-
weak inhibitor
benzoyl-CoA
-
-
Co2+
-
5 mM
Cu2+
-
5 mM
diethyl dicarbonate
diphosphate
-
weak inhibitor
Fe2+
-
5 mM
Mn2+
-
5 mM
N-bromosuccinimide
Ni2+
-
5 mM
Triton X-100
50% inhibition
Tween 80
60% inhibition
Zn2+
-
5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.112
2,4,5,6-tetrachloroisophthalonitrile
pH 7.0, 50°C
0.0104
2,4-Dichlorobenzoyl-CoA
-
-
0.042
3,4-dichlorobenzoyl-CoA
-
-
0.0042 - 0.036
4-bromobenzoyl-CoA
0.024
4-bromophenacyl-CoA
-
wild-type enzyme, pH 7.5, 25°C
0.03
4-chloro-2-nitrobenzoyl-CoA
-
-
0.075
4-chloro-3-methylbenzoyl-CoA
-
-
0.0055
4-chloro-3-nitrobenzoyl-CoA
-
-
0.02
4-chlorobenzoyl-3'-dephospho-CoA
-
wild-type enzyme, pH 7.5, 25°C
0.0024 - 0.11
4-chlorobenzoyl-CoA
0.033
4-chlorobenzoyl-dithio-CoA
-
wild-type enzyme, pH 7.5, 25°C
0.31
4-chlorobenzoyl-epsilon-CoA
-
wild-type enzyme, pH 7.5, 25°C
0.07 - 2
4-chlorobenzoyl-pantetheine
0.44
4-chlorobenzoyl-pantetheine phosphate
-
wild-type enzyme, pH 7.5, 25°C
0.04 - 0.075
4-fluorobenzoyl-CoA
0.0065 - 0.014
4-iodobenzoyl-CoA
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
207
2,4,5,6-tetrachloroisophthalonitrile
Pseudomonas sp.
C7EW69
pH 7.0, 50°C
0.511
2,4-Dichlorobenzoyl-CoA
Pseudomonas sp.
-
-
0.052
3,4-dichlorobenzoyl-CoA
Pseudomonas sp.
-
-
1.4 - 2.4
4-bromobenzoyl-CoA
0.03
4-bromophenacyl-CoA
Pseudomonas sp.
-
wild-type enzyme, pH 7.5, 25°C
0.063
4-chloro-2-nitrobenzoyl-CoA
Pseudomonas sp.
-
-
0.45
4-chlorobenzoyl-3'-dephospho-CoA
Pseudomonas sp.
-
wild-type enzyme, pH 7.5, 25°C
0.0000076 - 5
4-chlorobenzoyl-CoA
0.003
4-chlorobenzoyl-dithio-CoA
Pseudomonas sp.
-
wild-type enzyme, pH 7.5, 25°C
0.007
4-chlorobenzoyl-epsilon-CoA
Pseudomonas sp.
-
wild-type enzyme, pH 7.5, 25°C
0.001 - 0.056
4-chlorobenzoyl-pantetheine
0.051
4-chlorobenzoyl-pantetheine phosphate
Pseudomonas sp.
-
wild-type enzyme, pH 7.5, 25°C
0.003
4-fluorobenzoyl-CoA
Arthrobacter sp.
-
-
1.1 - 2
4-iodobenzoyl-CoA
0.6 - 2
chlorobenzoyl-CoA
additional information
additional information
Pseudomonas sp.
-
turnover rates for dormations of intermediates, wildtype and mutant
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.185
2,4,5,6-tetrachloroisophthalonitrile
Pseudomonas sp.
C7EW69
pH 7.0, 50°C
42259
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.77
3'-Dephospho-CoA
-
wild-type enzyme, pH 7.5, 25°C
21
4-Chlorobenzoate
-
wild-type enzyme, pH 7.5, 25°C
0.055
4-chlorobenzoyl-coenzyme A
-
wild-type enzyme, pH 7.5, 25°C
0.0017 - 0.1
4-hydroxybenzoyl-CoA
0.069
4-hydroxybenzoyl-dithio-CoA
-
wild-type enzyme, pH 7.5, 25°C
0.022
4-methylbenzoyl-3'-dephospho-CoA
-
wild-type enzyme, pH 7.5, 25°C
0.0031 - 0.072
4-methylbenzoyl-CoA
4.2
5'-ADP
-
wild-type enzyme, pH 7.5, 25°C
0.09 - 2.4
CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.007
-
time elapsed at 45°C, 1020 min, recovery 1.7%
0.08
-
time elapsed at 45°C, 120 min, recovery 19.9%
0.082
-
time elapsed at 45°C, 0 min, recovery 20.4%; time elapsed at 45°C, 15 min, recovery 20.4%; time elapsed at 45°C, 5 min, recovery 20.4%
0.194
-
renaturation of 4-CBCoA dehalogenaase following exposure to elevated temperature, 55°C, activity after heating to 60°C 0.081, recovery 20.1%
0.243
-
renaturation of 4-CBCoA dehalogenaase following exposure to elevated temperature, 20°C, activity after heating to 60°C 0.038, recovery 9.5%
0.301
-
renaturation of 4-CBCoA dehalogenaase following exposure to elevated temperature, 30°C, activity after heating to 60°C 0.051, recovery 12.7%
0.349
-
renaturation of 4-CBCoA dehalogenaase following exposure to elevated temperature, 50°C, activity after heating to 60°C 0.082, recovery 20.4%
0.36
-
renaturation of 4-CBCoA dehalogenaase following exposure to elevated temperature, 40°C, activity after heating to 60°C 0.055, recovery 13.7%
0.363
-
renaturation of 4-CBCoA dehalogenaase after return from pH 5.2 to pH 7.4, incubation time 7 min, recovery 89%
0.365
-
renaturation of 4-CBCoA dehalogenaase after return from pH 10.1 to pH 7.4, incubation time 7 min, recovery 90%
0.402
-
renaturation of 4-CBCoA dehalogenaase following exposure to elevated temperature, 45°C, activity after heating to 60°C 0.083, recovery 20.6%
0.407
-
renaturation of 4-CBCoA dehalogenaase after return from pH 10.1 to pH 7.4, incubation time 17 min, recovery 99%
0.41
-
pH 7.4; renaturation of 4-CBCoA dehalogenaase after return from pH 5.2 to pH 7.4, incubation time 17 min, recovery 100%
1.5
-
purified wild-type enzyme
3.61
-
pH 7.5, 30°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.3
-
pH 6.0: about 55% of maximal activity, pH 9.3: about 55% of maximal activity
7.4
-
when incubated for 5 Min at 1.5 mg ml-1 in buffer at 5.2 or 10.1 enzyme activity is lost completely
9 - 11.5
-
about 50% of maximal activity at pH 9.0 and at pH 11.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
activity assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 55
-
15°C: about 50% of maximal activity, 55°C: about 50% of maximal activity
30 - 65
-
about 60% of maximal activity at 30°C and at 65°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.13
sequence calculation
6.4
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29847
-
4 * 29847, calculation from nucleotide sequence
33000
-
4 * 33000, SDS-PAGE
33886
1 x 36000, SDS-PAGE, 1 * 33886, mass spectrometry
122000
-
gel filtration
131000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
multimer
octamer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant H90Q complexed with the substrate, 8% PEG 8000, 0.2 M potassium chloride, 50 mM CHES, pH 9.0, 5 mM NaN3, 4 °C, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
three-dimensional structure
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
10 min, complete loss of activity
33082
6 - 9
purified Chd, 95% activity remaining after 30 min
719717
6
-
60 min, 10% loss of activity
33082
6.5 - 10
-
4°C, 4 h, stable
33077
6.5
-
irreversible inactivation below
33077
6.5 - 11
-
60 min, stable
33082
11.5
-
60 min, 10% loss of activity
33082
12
-
10 min, complete loss of activity
33082
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
Chd is fairly stable up to
65
-
15 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pure enzyme is completely inactive after a single freeze and thawing cycle
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, impure preparations, stable for several months
-
-20°C, purified enzyme,50 mM PBS, pH 7.0, 10% glycerol, no loss of Chd activity within 3 months
4°C, purified enzyme, 3-5% of Chd activity is lost within 8 weeks
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-CBCoA dehalogenase is purified to homogeneity from cells of Arthrobacter sp. strain TM-1
-
recombinant enzyme
recombinant wild-type and mutants from Escherichia coli, to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, recombinant expression
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli
-
gene fcbB, partial DNA and amino acid sequence determination and analysis
-
overexpression of wild-type and mutants in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A112S
-
site-directed mutagenesis, overexpression as insoluble protein
A112V
-
site-directed mutagenesis, overexpression as soluble protein, reduced activity
D130A
site-directed mutagenesis, inactive mutant
D145A
-
mutant enzymes D145A and H90Q show no catalytic activity, but no effect on ligand binding or the induction of the red shift in the benzoyl ring absorption
D184A
site-directed mutagenesis, inactive mutant
D337A
site-directed mutagenesis, the Km for the mutant Chd increases to 0.176 mM, 50% transformation activity compared to the wild-type Chd
D45A
site-directed mutagenesis, inactive mutant
E232D
-
mutant enzyme binds the substrate analogue 4-methylbenzoyl-CoA more tightly than does the wild-type dehalogenase. The kcat for 4-chlorobenzoyl-CoS conversion to product is reduced 10000fold in the mutant. Increased sibstrate binding, decreased ring polarization, and decreased catalytic efficiency indicate that the repositioning of the point charge in the Glu232Arg mutant might affect the orientation of the Arg145 carboxylate with respect to the aromatic ring
F64A
-
site-directed mutagenesis, decreased kcat and slightly increased Km compared to the wild-type enzyme
F64L
-
The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
F82L
-
The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
G113N
-
site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
G113S
-
site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
G114A
-
The G114A mutant is strongly inhibited in both substrate binding and activation
G115L
-
site-directed mutagenesis, overexpression as insoluble protein
G115N
-
site-directed mutagenesis, overexpression as insoluble protein
G115S
-
site-directed mutagenesis, overexpression as insoluble protein
G115V
-
site-directed mutagenesis, overexpression as insoluble protein
G63A
-
site-directed mutagenesis, overexpression as insoluble protein
G63I
-
site-directed mutagenesis, overexpression as insoluble protein
G63P
-
site-directed mutagenesis, overexpression as insoluble protein
H128Q
site-directed mutagenesis, inactive mutant
H157Q
site-directed mutagenesis, inactive mutant
H63Q
site-directed mutagenesis, the Km for the mutant Chd increases to 0.154 mM compared to the wild-type
H81Q
-
mutant enzymes H81Q, W137F and H90Q show significant loss in catalytic activity
H94Q
-
The mutant enzymes H94Q, H208Q, and W179F have a catalytic activity comparable to the wild-type enzyme
R24K
-
site-directed mutagenesis, increased kcat and increased Km compared to the wild-type enzyme
R24L
-
site-directed mutagenesis, decreased kcat and increased Km compared to the wild-type enzyme
R257K
-
site-directed mutagenesis, slightly decreased kcat and slightly increased Km compared to the wild-type enzyme
R257L
-
site-directed mutagenesis, decreased kcat and increased Km compared to the wild-type enzyme
R67K
-
site-directed mutagenesis, decreased kcat and slightly increased Km compared to the wild-type enzyme
R67L
-
site-directed mutagenesis, expression in inclusion bodies
W89F
-
The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
W89Y
-
The W89Y mutant is inhibited in catalysis and ligand binding
Y65D
-
site-directed mutagenesis, overexpression as soluble protein, slightly reduced activity
F64L
-
The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
-
F64P
-
site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
-
F82L
-
The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
-
G113A
-
site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
-
G113S
-
site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
-
G114A
-
The G114A mutant is strongly inhibited in both substrate binding and activation
-
G115S
-
site-directed mutagenesis, overexpression as insoluble protein
-
G63A
-
site-directed mutagenesis, overexpression as insoluble protein
-
W137F
-
structure and reaction simulations compared to the wild-type enzyme
-
W89F
-
The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
-
W89Y
-
The W89Y mutant is inhibited in catalysis and ligand binding
-
D130A
-
site-directed mutagenesis, inactive mutant
-
D184A
-
site-directed mutagenesis, inactive mutant
-
D337A
-
site-directed mutagenesis, the Km for the mutant Chd increases to 0.176 mM, 50% transformation activity compared to the wild-type Chd
-
D45A
-
site-directed mutagenesis, inactive mutant
-
H157Q
-
site-directed mutagenesis, inactive mutant
-
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
denaturation and renaturation experiments as functions of pH and temperature are performed
-
Show AA Sequence (165 entries)
Please use the Sequence Search for a specific query.