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Information on EC 3.8.1.7 - 4-chlorobenzoyl-CoA dehalogenase
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3.8.1.7 4-chlorobenzoyl-CoA dehalogenaseIUBMB Comments
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.
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Word Map
- 3.8.1.7
-
dehalogenation
- 4-hydroxybenzoyl-coa
-
meisenheimer
- 4-hydroxybenzoate
-
thioesterase
-
4-hba-coa
-
raman
- arthrobacter
-
dechlorination
-
dunaway-mariano
-
homotetramer
-
expulsion
-
pi-electrons
-
4-position
- crotonase
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
4-chlorobenzoyl-coa dehalogenase, 4-cba-coa dehalogenase, 4-chlorobenzoyl-coenzyme a dehalogenase, 4-chlorobenzoyl coa dehalogenase, 4-chlorobenzoate-coenzyme a dehalogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-CBA-CoA dehalogenase
4-CBS-CoA dehalogenase
-
-
-
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4-chlorobenzoate-CoA-dehalogenase
4-chlorobenzoate-coenzyme A dehalogenase
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-
-
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4-chlorobenzoyl CoA dehalogenase
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-
-
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4-chlorobenzoyl-CoA dehalogenase
4-chlorobenzoyl-coenzyme A dehalogenase
CHD
dehalogenase, 4-chlorobenzoyl coenzyme A
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-
-
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dehalogenase, 4-chlorobenzoyl coenzyme A (Pseudomonas strain CBS-3 clone pMMB22 reduced)
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-
-
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4-chlorobenzoyl-CoA dehalogenase
-
-
-
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4-chlorobenzoyl-coenzyme A dehalogenase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
formation of an aryl intermediate
-
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
it is proposed that Asp125 functions as the active site nucleophile, that Trp137 serves as a hydrogen bond donor to the Asp145 carbonyl group , and that His90 serves to deprotonate the bound H2O molecule
-
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
Asp145 provides the side-chain carboxylate group that adds to form the Meisenheimer intermediate and His90 serves as the general base in the subsequent hydrolysis step
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
formation of an aryl-enzyme intermediate that is converted to a hydroxamic acid upon attack by hydroxylamine. The dehalogenation appears to occur via an SNAr mechanism
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4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
specific for dehalogenation at the 4-position, can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position, mechanism, Asp145 acts as a nucleophil on the C(4) of the substrates' benzoyl ring to form a Meisenheimer intermediate, followed by expulsion of chloride ion to form an arylated enzyme intermediate, and ester hydrolysis to form 4-hydroxybenzoyl-CoA, active site structure
-
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
specific for dehalogenation at the 4-position, can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position, mechanism, attack of Asp145 on the C(4) of the substrates' benzoyl ring to form a Meisenheimer intermediate, followed by expulsion of chloride ion to form an arylated enzyme intermediate, and ester hydrolysis to form 4-hydroxybenzoyl-CoA, active site residue His90 is involved and important for the regeneration of the active enzyme
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
specific for dehalogenation at the 4-position, can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position, multistep mechanism, attack of Asp145 on the C(4) of the substrates' benzoyl ring to form a Meisenheimer intermediate, followed by expulsion of chloride ion to form an arylated enzyme intermediate, and ester hydrolysis to form 4-hydroxybenzoyl-CoA, active site structure
-
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
specific for dehalogenation at the 4-position, can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position, SNAr mechanism
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4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
specific for dehalogenation at the 4-position, can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position, SNAr reaction mechanism, the substrate is bound in the active site primariliy formed by 2 of 3 subunits, reaction is initiated by the nucleophilic attack at the C4 of the benzoyl group of the substrate by carboxylate of Asp145 to form a Meisenheimer intermediate, general base for the hydrolysis is His90, the benzoyl group is surrounded by F64, F82, W89, and W137, active site conformations of wild-type and mutant W137F
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4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
formation of an aryl-enzyme intermediate that is converted to a hydroxamic acid upon attack by hydroxylamine. The dehalogenation appears to occur via an SNAr mechanism
-
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4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
specific for dehalogenation at the 4-position, can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position, mechanism, Asp145 acts as a nucleophil on the C(4) of the substrates' benzoyl ring to form a Meisenheimer intermediate, followed by expulsion of chloride ion to form an arylated enzyme intermediate, and ester hydrolysis to form 4-hydroxybenzoyl-CoA, active site structure
-
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4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
specific for dehalogenation at the 4-position, can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position, SNAr reaction mechanism, the substrate is bound in the active site primariliy formed by 2 of 3 subunits, reaction is initiated by the nucleophilic attack at the C4 of the benzoyl group of the substrate by carboxylate of Asp145 to form a Meisenheimer intermediate, general base for the hydrolysis is His90, the benzoyl group is surrounded by F64, F82, W89, and W137, active site conformations of wild-type and mutant W137F
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4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
Asp145 provides the side-chain carboxylate group that adds to form the Meisenheimer intermediate and His90 serves as the general base in the subsequent hydrolysis step
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-
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-halide hydrolysis
dehalogenation
hydrolysis of C-halide
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-
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-
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PATHWAY SOURCE
PATHWAYS
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-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
141583-18-8
-
141955-45-5
dehalogenase, 4-chlorobenzoyl coenzyme A (Pseudomonas strain CBS-3 clone pMMB22 reduced)
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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
2,4,5,6-tetrachloroisophthalonitrile + H2O
4-hydroxy-trichloroisophthalonitrile + chloride
4-chlorobenzoyl-3'-dephospho-CoA + H2O
4-hydroxybenzoyl-3'-dephospho-CoA + chloride
-
-
-
-
?
4-chlorobenzoyl-dithio-CoA + H2O
4-hydroxybenzoyl-dithio-CoA + chloride
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-
-
-
?
4-chlorobenzoyl-epsilon-CoA + H2O
4-hydroxybenzoyl-epsilon-CoA + chloride
-
-
-
-
?
4-chlorobenzoyl-pantetheine + H2O
4-hydroxybenzoyl-pantetheine + chloride
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very low activity
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-
?
4-chlorobenzoyl-pantetheine phosphate + H2O
4-hydroxybenzoyl-pantetheine phosphate + chloride
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-
-
-
?
2,4,5,6-tetrachloroisophthalonitrile + H2O
4-hydroxy-trichloroisophthalonitrile + chloride
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-
-
?
2,4,5,6-tetrachloroisophthalonitrile + H2O
4-hydroxy-trichloroisophthalonitrile + chloride
a regiospecific hydroxyl substitution at the 4-chlorine atom of chlorothalonil. Histidines 128 and 157, serine 126, aspartates 45, 130 and 184, and tryptophan 241 are essential for the dehalogenase activity
product identified by reverse-phase HPLC, tandem mass spectrometry, and NMR
-
?
2,4,5,6-tetrachloroisophthalonitrile + H2O
4-hydroxy-trichloroisophthalonitrile + chloride
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-
-
?
2,4,5,6-tetrachloroisophthalonitrile + H2O
4-hydroxy-trichloroisophthalonitrile + chloride
a regiospecific hydroxyl substitution at the 4-chlorine atom of chlorothalonil. Histidines 128 and 157, serine 126, aspartates 45, 130 and 184, and tryptophan 241 are essential for the dehalogenase activity
product identified by reverse-phase HPLC, tandem mass spectrometry, and NMR
-
?
4-bromobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + bromide
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-
-
-
?
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
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-
-
?
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
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-
-
-
?
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
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the variant W137A binds the product 4-hydroxybenzoyl in two conformational states in the active site. In these two forms the 4-hydroxybenzoyl moiety is experiencing modest and very strong electron electron polarizing environments. The two forms may be interconverted by varying the temperature
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?
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
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degradation in soil, pathway overview
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-
?
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
electrostatic influence of active-site waters on the nucleophilic aromatic substitution catalyzed by 4-chlorobenzoyl-CoA dehalogenase. A quantum mechanical/molecular mechanical simulation of the potential of mean force for the substitution step conforms the increased barrier height in the H90Q mutant and provides the increased barrier height in the H90Q mutant and provides evidence on the electrostatic influence of two-site waters on the rate-limiting barrier
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-
?
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
reaction rate is limited by the formation of the Meisenheimer comlex, rather than by its decomposition
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-
?
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
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-
-
-
?
4-fluorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + fluoride
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weak activity
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-
?
4-fluorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + fluoride
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weak activity
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-
?
4-fluorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + fluoride
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no activity
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-
?
4-iodobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + iodide
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-
-
-
?
additional information
?
-
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no activity with 3-chlorobenzoyl-CoA and 2-chlorobenzoyl-CoA
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-
?
additional information
?
-
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no activity with 3-chlorobenzoyl-CoA and 2-chlorobenzoyl-CoA
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-
?
additional information
?
-
no activity with chlorobenzene, 4-dichlorobenzene, 4-chloronitrobenzene, pentachloronitrobenzene, 4-chlorobenzoate, 4-chlorophenylacetic acid, 3-chloroaniline, 4-chloroaniline, and pentachlorophenol
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-
?
additional information
?
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no activity with chlorobenzene, 4-dichlorobenzene, 4-chloronitrobenzene, pentachloronitrobenzene, 4-chlorobenzoate, 4-chlorophenylacetic acid, 3-chloroaniline, 4-chloroaniline, and pentachlorophenol
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-
?
additional information
?
-
no activity with chlorobenzene, 4-dichlorobenzene, 4-chloronitrobenzene, pentachloronitrobenzene, 4-chlorobenzoate, 4-chlorophenylacetic acid, 3-chloroaniline, 4-chloroaniline, and pentachlorophenol
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-
?
additional information
?
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degradation via the stages of formation of intermediates, 4-hydroxybenzoate and protocatechuic acid, to compounds of the basic metabolism is controlled by the fcbA and fcbB genes encoding 4-chlorobenzoate-CoA ligase and 4-chlorobenzoate-CoA-dehalogenase, respectively, overview
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-
?
additional information
?
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degradation via the stages of formation of intermediates, 4-hydroxybenzoate and protocatechuic acid, to compounds of the basic metabolism is controlled by the fcbA and fcbB genes encoding 4-chlorobenzoate-CoA ligase and 4-chlorobenzoate-CoA-dehalogenase, respectively, overview
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-
?
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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
2,4,5,6-tetrachloroisophthalonitrile + H2O
4-hydroxy-trichloroisophthalonitrile + chloride
2,4,5,6-tetrachloroisophthalonitrile + H2O
4-hydroxy-trichloroisophthalonitrile + chloride
-
-
-
?
2,4,5,6-tetrachloroisophthalonitrile + H2O
4-hydroxy-trichloroisophthalonitrile + chloride
-
-
-
?
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
-
degradation in soil, pathway overview
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-
?
4-chlorobenzoyl-CoA + H2O
4-hydroxybenzoyl-CoA + chloride
-
-
-
-
?
additional information
?
-
-
degradation via the stages of formation of intermediates, 4-hydroxybenzoate and protocatechuic acid, to compounds of the basic metabolism is controlled by the fcbA and fcbB genes encoding 4-chlorobenzoate-CoA ligase and 4-chlorobenzoate-CoA-dehalogenase, respectively, overview
-
-
?
additional information
?
-
-
degradation via the stages of formation of intermediates, 4-hydroxybenzoate and protocatechuic acid, to compounds of the basic metabolism is controlled by the fcbA and fcbB genes encoding 4-chlorobenzoate-CoA ligase and 4-chlorobenzoate-CoA-dehalogenase, respectively, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Chd dehalogenates chlorothalonil under anaerobic and aerobic conditions and does not require the presence of cofactors such as CoA and ATP
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additional information
-
Chd dehalogenates chlorothalonil under anaerobic and aerobic conditions and does not require the presence of cofactors such as CoA and ATP
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
no activating effects by Cu2+, Ba2+, Mg2+, or Ni2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
complete inhibition, recovered by the subsequent supplementation with Zn2+
diethyl dicarbonate
-
activity is fully regained by subsequent treatment with hydroxylamine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
4-chlorobenzoyl-pantetheine
-
wild-type enzyme, pH 7.5, 25°C, in presence of 1 mM 5'-ADP
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
turnover rates for dormations of intermediates, wildtype and mutant
-
0.0002
4-chlorobenzoyl-CoA
multiple turnovers, mutant H90Q, pH 7.5, 25°C
0.7
4-chlorobenzoyl-CoA
multiple turnovers, wild-type enzyme, pH 7.5, 25°C
2.3
4-chlorobenzoyl-CoA
single turnover, wild-type enzyme, pH 7.5, 25°C
0.056
4-chlorobenzoyl-pantetheine
-
wild-type enzyme, pH 7.5, 25°C, in presence of 1 mM 5'-ADP
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kcat/KM VALUE [1/mMs-1]
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
0.082
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
additional information
0.41
-
renaturation of 4-CBCoA dehalogenaase after return from pH 5.2 to pH 7.4, incubation time 17 min, recovery 100%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
45
45
-
activity is maximal at 45°C and is totally lost by heating to 60°C for 5 min
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 55
-
15°C: about 50% of maximal activity, 55°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a 2,4,5,6-tetrachloroisophthalonitrile (chlorothalonil)-degrading strain
UniProt
brenda
a 2,4,5,6-tetrachloroisophthalonitrile (chlorothalonil)-degrading strain
UniProt
brenda
wild-type and mutant enzymes D145A, H90Q, W137F, W89F, W89Y, F64L, F82L, G114A
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
strain P25 utilizes 4-chlorobiphenyl and 4-chlorobenzoic acid as sole carbon and energy sources
brenda
-
strain P25 utilizes 4-chlorobiphenyl and 4-chlorobenzoic acid as sole carbon and energy sources
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
evolution
Chd contains a putative conserved domain of the metallo-beta-lactamase superfamily and shows the highest identity with several metallohydrolases
evolution
-
Chd contains a putative conserved domain of the metallo-beta-lactamase superfamily and shows the highest identity with several metallohydrolases
-
metabolism
-
the organism catalyzes the initial dehalogenation reaction of 4-chlorobenzoic acid degeneration via the stages of formation of intermediates, 4-hydroxybenzoate and protocatechuic acid, to compounds of the basic metabolism, also involvement of protocatechuate 4,5-dioxygenase, overview
metabolism
-
the organism catalyzes the initial dehalogenation reaction of 4-chlorobenzoic acid degeneration via the stages of formation of intermediates, 4-hydroxybenzoate and protocatechuic acid, to compounds of the basic metabolism, also involvement of protocatechuate 4,5-dioxygenase, overview
-
Show AA Sequence and Transmembrane Helices (344 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
30000
31000
31000
-
4 * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
31000
-
8 * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
31000
-
x * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
multimer
octamer
tetramer
multimer
-
x * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
multimer
-
x * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
-
octamer
-
8 * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
octamer
-
8 * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
-
tetramer
-
4 * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
tetramer
-
4 * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
-
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A112V
-
site-directed mutagenesis, overexpression as soluble protein, reduced activity
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
D337A
site-directed mutagenesis, the Km for the mutant Chd increases to 0.176 mM, 50% transformation activity compared to the wild-type Chd
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
F64P
F82L
-
The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
G113A
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
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
H90Q
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
W137F
W89F
-
The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
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
-
W89F
-
The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
-
D337A
-
site-directed mutagenesis, the Km for the mutant Chd increases to 0.176 mM, 50% transformation activity compared to the wild-type Chd
-
F64P
-
site-directed mutagenesis, highly decreased kcat compared to the wild-type enzyme, nearly inactive
F64P
-
site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
G113A
-
site-directed mutagenesis, decreased kcat and increased Km compared to the wild-type enzyme
G113A
-
site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
G113A
mutation significantly increases the barrier by disrupting the hydrogen bond with the Gly114 backbone
H90Q
-
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
H90Q
site-directed mutagenesis, exchange of the active site H90, reduced formation of arylated enzyme intermediate, and 154fold reduction of arylated enzyme intermediate hydrolysis, active site structure
W137F
-
mutant enzymes H81Q, W137F and H90Q show significant loss in catalytic activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
50
purified enzyme, 95% activity remaining after 10 min, 18% after 1 h
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified enzyme,50 mM PBS, pH 7.0, 10% glycerol, no loss of Chd activity within 3 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
4-CBCoA dehalogenase is purified to homogeneity from cells of Arthrobacter sp. strain TM-1
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, recombinant expression
gene fcbB, partial DNA and amino acid sequence determination and analysis
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation and renaturation experiments as functions of pH and temperature are performed
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chang, K.H.; Liang, P.H.; Beck, W.; Scholten, J.D.; Dunaway-Mariano, D.
Isolation and characterization of the three polypeptide components of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3
Biochemistry
31
5605-5610
1992
Pseudomonas sp., Pseudomonas sp. CBS-3
brenda
Dunaway-Mariano, D.; Babbitt, P.C.
On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway
Biodegradation
5
259-276
1994
Arthrobacter sp., Pseudomonas sp., Arthrobacter sp. 4-CB1, Pseudomonas sp. CBS-3
brenda
Crooks, G.P.; Copley, S.D.
Purification and characterization of 4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain 4-CB1
Biochemistry
33
11645-11649
1994
Arthrobacter sp., Arthrobacter sp. 4-CB1
brenda
Liang, P.H.; Yang, G.; Dunaway-Mariano, D.
Specificity of 4-chlorobenzoyl coenzyme A dehalogenase catalyzed dehalogenation of halogenated aromatics
Biochemistry
32
12245-12250
1993
Pseudomonas sp., Pseudomonas sp. CBS-3
brenda
Taylor, K.L.; Xiang, H.; Liu, R.Q.; Yang, G.; Dunaway-Mariano, D.
Investigation of substrate activation by 4-chlorobenzoyl-coenzyme A dehalogenase
Biochemistry
36
1349-1361
1997
Pseudomonas sp., Pseudomonas sp. CBS-3
brenda
Benning, M.M.; Taylor, K.L.; Liu, R.Q.; Yang, G.; Xiang, H.; Wesenberg, G.; Dunaway-Mariano, D.; Holden, H.M.
Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 A resolution: an enzyme catalyst generated via adaptive mutation
Biochemistry
35
8103-8109
1996
Pseudomonas sp. (A5JTM5), Pseudomonas sp., Pseudomonas sp. CBS-3 (A5JTM5)
brenda
Lffler, F.; Lingens, F.; Muller, R.
Dehalogenation of 4-chlorobenzoate. Characterisation of 4-chlorobenzoyl-coenzyme A dehalogenase from Pseudomonas sp. CBS3
Biodegradation
6
203-212
1995
Pseudomonas sp., Pseudomonas sp. CBS-3
brenda
Yang, G.; Liang, P.H.; Dunaway-Mariano, D.
Evidence for nucleophilic catalysis in the aromatic substitution reaction catalyzed by 4-chlorobenzoyl-coenzyme A dehalogenase
Biochemistry
33
8527-8531
1994
Pseudomonas sp.
brenda
Yang, G.; Liu, R.Q.; Taylor, K.L.; Xiang, H.; Price, J.; Dunaway-Mariano, D.
Identification of active site residues essential to 4-chlorobenzoyl-coenzyme A dehalogenase catalysis by chemical modification and site directed mutagenesis
Biochemistry
35
10879-10885
1996
Pseudomonas sp.
brenda
Crooks, G.P.; Xu, L.; Barkley, R.M.; Copley, S.D.
Exploration of possible mechanisms for 4-chlorobenzoyl CoA dehalogenase: evidence for an aryl-enzyme intermediate
J. Am. Chem. Soc.
117
10791-10798
1995
Arthrobacter sp., Arthrobacter sp. 4-CB1
-
brenda
Zhang, W.; Wei, Y.; Luo, L.; Taylor, K.L.; Yang, G.; Dunaway-Mariano, D.; Benning, M.M.; Holden, H.M.
Histidine 90 function in 4-chlorobenzoyl-coenzyme A dehalogenase catalysis
Biochemistry
40
13474-13482
2001
Pseudomonas sp. (A5JTM5)
brenda
Luo, L.; Taylor, K.L.; Xiang, H.; Wei, Y.; Zhang, W.; Dunaway-Mariano, D.
Role of active site binding interactions in 4-chlorobenzoyl-coenzyme A dehalogenase catalysis
Biochemistry
40
15684-15692
2001
Pseudomonas sp.
brenda
Dong, J.; Lu, X.; Wei, Y.; Luo, L.; Dunaway-Mariano, D.; Carey, P.R.
The strength of dehalogenase-substrate hydrogen bonding correlates with the rate of Meisenheimer intermediate formation
Biochemistry
42
9482-9490
2003
Pseudomonas sp., Pseudomonas sp. CBS-3
brenda
Xu, D.; Guo, H.; Gao, J.; Cui, Q.
A QM/MM study of a nucleophilic aromatic substitution reaction catalyzed by 4-chlorobenzoyl-CoA dehalogenase
Chem. Commun. (Camb.)
2004
892-893
2004
Bacteria
-
brenda
Lau, E.Y.; Bruice, T.C.
The active site dynamics of 4-chlorobenzoyl-CoA dehalogenase
Proc. Natl. Acad. Sci. USA
98
9527-9532
2001
Pseudomonas sp., Pseudomonas sp. CBS-3
brenda
Zhou, L.; Marks, T.S.; Poh, R.P.; Smith, R.J.; Chowdhry, B.Z.; Smith, A.R.
The purification and characterisation of 4-chlorobenzoate:CoA ligase and 4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain TM-1
Biodegradation
15
97-109
2004
Arthrobacter sp., Arthrobacter sp. TM-1
brenda
Wu, J.; Xu, D.; Lu, X.; Wang, C.; Guo, H.; Dunaway-Mariano, D.
Contributions of long-range electrostatic interactions to 4-chlorobenzoyl-CoA dehalogenase catalysis: a combined theoretical and experimental study
Biochemistry
45
102-112
2006
Pseudomonas sp.
brenda
Xu, D.; Guo, H.
Electrostatic influence of active-site waters on the nucleophilic aromatic substitution catalyzed by 4-chlorobenzoyl-CoA dehalogenase
FEBS Lett.
579
4249-4253
2005
Pseudomonas sp. (A5JTM5)
brenda
Xu, D.; Wei, Y.; Wu, J.; Dunaway-Mariano, D.; Guo, H.; Cui, Q.; Gao, J.
QM/MM studies of the enzyme-catalyzed dechlorination of 4-chlorobenzoyl-CoA provide insight into reaction energetics
J. Am. Chem. Soc.
126
13649-13658
2004
Pseudomonas sp. (A5JTM5)
brenda
Dong, J.; Luo, L.; Dunaway-Mariano, D.; Carey, P.R.
Raman evidence for product binding to the enzyme W137F 4-chlorobenzoyl-CoA dehalogenase in two conformational states
J. Raman Spectros.
36
320-325
2005
Pseudomonas sp.
-
brenda
Zhou, L.; Poh, R.P.; Marks, T.S.; Chowdhry, B.Z.; Smith, A.R.
Structure and denaturation of 4-chlorobenzoyl coenzyme A dehalogenase from Arthrobacter sp. strain TM-1
Biodegradation
19
65-75
2008
Arthrobacter sp.
brenda
Chae, J.C.; Song, B.; Zylstra, G.J.
Identification of genes coding for hydrolytic dehalogenation in the metagenome derived from a denitrifying 4-chlorobenzoate degrading consortium
FEMS Microbiol. Lett.
281
203-209
2008
consortium cosmid clone pGZ1
brenda
Wang, G.; Li, R.; Li, S.; Jiang, J.
A novel hydrolytic dehalogenase for the chlorinated aromatic compound chlorothalonil
J. Bacteriol.
192
2737-2745
2010
Pseudomonas sp. (C7EW69), Pseudomonas sp., Pseudomonas sp. CTN-3 (C7EW69)
brenda
Plotnikova, E.; Solyanikova, I.; Egorova, D.; Shumkova, E.; Golovleva, L.
Degradation of 4-chlorobiphenyl and 4-chlorobenzoic acid by the strain Rhodococcus ruber P25
Microbiology
81
143-153
2012
Rhodococcus ruber, Rhodococcus ruber P25
brenda
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