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Information on EC 3.8.1.7 - 4-chlorobenzoyl-CoA dehalogenase and Organism(s) Pseudomonas sp. and UniProt Accession A5JTM5
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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 taxonomic range for the selected organisms is: Pseudomonas sp.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-CBS-CoA dehalogenase
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4-chlorobenzoate-coenzyme A dehalogenase
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4-chlorobenzoyl CoA dehalogenase
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4-chlorobenzoyl-CoA dehalogenase
4-chlorobenzoyl-coenzyme A dehalogenase
dehalogenase, 4-chlorobenzoyl coenzyme A
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dehalogenase, 4-chlorobenzoyl coenzyme A (Pseudomonas strain CBS-3 clone pMMB22 reduced)
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4-chlorobenzoyl-CoA dehalogenase
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4-chlorobenzoyl-coenzyme A dehalogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
formation of an aryl intermediate
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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
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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, 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
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-halide
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY
141583-18-8
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141955-45-5
dehalogenase, 4-chlorobenzoyl coenzyme A (Pseudomonas strain CBS-3 clone pMMB22 reduced)
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
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-
-
-
?
4-chlorobenzoyl-dithio-CoA + H2O
4-hydroxybenzoyl-dithio-CoA + chloride
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-
-
-
?
4-chlorobenzoyl-epsilon-CoA + H2O
4-hydroxybenzoyl-epsilon-CoA + chloride
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-
-
-
?
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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-
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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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-
?
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
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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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?
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
?
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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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?
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
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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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?
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
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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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
complete inhibition, recovered by the subsequent supplementation with Zn2+
diethyl dicarbonate
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activity is fully regained by subsequent treatment with hydroxylamine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
4-chlorobenzoyl-pantetheine
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wild-type enzyme, pH 7.5, 25°C, in presence of 1 mM 5'-ADP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
turnover rates for dormations of intermediates, wildtype and mutant
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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
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wild-type enzyme, pH 7.5, 25°C, in presence of 1 mM 5'-ADP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Chd contains a putative conserved domain of the metallo-beta-lactamase superfamily and shows the highest identity with several metallohydrolases
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
31000
31000
-
4 * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
31000
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8 * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
31000
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x * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
multimer
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x * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
octamer
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8 * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
tetramer
tetramer
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4 * 31000, the enzyme is active in tetrameric, octameric and higher multimeric forms, SDS-PAGE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G113A
mutation significantly increases the barrier by disrupting the hydrogen bond with the Gly114 backbone
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
A112V
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site-directed mutagenesis, overexpression as soluble protein, reduced activity
D145A
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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
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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
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site-directed mutagenesis, decreased kcat and slightly increased Km compared to the wild-type enzyme
F64L
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The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
F64P
F82L
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The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
G113A
G113N
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site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
G113S
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site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
G114A
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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
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mutant enzymes H81Q, W137F and H90Q show significant loss in catalytic activity
H90Q
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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
H94Q
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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
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The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
Y65D
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site-directed mutagenesis, overexpression as soluble protein, slightly reduced activity
F64P
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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
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site-directed mutagenesis, decreased kcat and increased Km compared to the wild-type enzyme
G113A
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site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
W137F
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mutant enzymes H81Q, W137F and H90Q show significant loss in catalytic activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
50
purified enzyme, 95% activity remaining after 10 min, 18% after 1 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, recombinant expression
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
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., Arthrobacter sp. 4-CB1, Pseudomonas sp., Pseudomonas sp. CBS-3
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
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
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)
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
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.
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.
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)
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.
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
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
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.
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)
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)
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.
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