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Information on EC 6.2.1.33 - 4-chlorobenzoate-CoA ligase

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.33 4-chlorobenzoate-CoA ligase
IUBMB Comments
Requires Mg2+. This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
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This record set is specific for:
UNIPROT: Q8GN86
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Word Map
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The enzyme appears in viruses and cellular organisms
Synonyms
4-chlorobenzoate:coa ligase, 4-chlorobenzoyl-coa ligase, 4-chlorobenzoate:coenzyme a ligase, 4-halobenzoate-coenzyme a ligase, 4-cba:coa ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-chlorobenzoate:CoA ligase
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4-Chlorobenzoate:coenzyme A ligase
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4-CBA:CoA ligase
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-
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4-Chlorobenzoate:coenzyme A ligase
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-
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4-Chlorobenzoyl-CoA ligase
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-
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4-Chlorobenzoyl-coenzyme A ligase
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-
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4-Halobenzoate-coenzyme A ligase
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-
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Synthetase, 4-chlorobenzoyl coenzyme A
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formation of thioester
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-
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SYSTEMATIC NAME
IUBMB Comments
4-chlorobenzoate:CoA ligase
Requires Mg2+. This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
141583-20-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
show the reaction diagram
4-Methylbenzoate + CoA + ATP
4-Methylbenzoyl-CoA + AMP + diphosphate
show the reaction diagram
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
show the reaction diagram
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chlorophenacyl-CoA
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AMP
is a noncompetitive inhibitor versus ATP and an uncompetitive versus CoA
diphosphate
competitive versus ATP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
transient-state and steady-state kinetics of wild-type and mutant enzymes, overview
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
inhibition kinetics, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
mutant D402P
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8GN86_9BURK
504
0
54320
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant CBL bound to 4-chlorobenzoyl-AMP, hanging drop vapor diffusion at 4°C using 16-24% pentaerythritol propoxylate 426, and 0.1 M K+-HEPES, pH 6.5 or 6.75, and optimized via hanging drop vapor diffusion using 14-18% PEG 1000, 50-100 mM magnesium nitrate and 100 mM MOPS, pH 7.0, the cryoprotectant contains 24% pentaerythritol propoxylate 426, 24% ethylene glycol, and 0.1 M K+-HEPES, 1 mM ATP, and 1 mM 4-chlorobenzoate, X-ray diffraction structure determination and analysis at 2.0-2.25 A resolution, molecular replacement
purified recombinant enzyme, X-ray diffraction structure determination and analysis, modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D385A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E410A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F473A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzymem but increased kcat
G408A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H207A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H207F
site-directed mutagenesis,the mutant shows reduced activity compared to the wild-type enzyme
H207Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H254A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K477A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K492A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K492L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K492R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
M203A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N302A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R400A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R439A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R475A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R87A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S407A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T161A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T251A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T306A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T307A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W440A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, but increased kcat
Y304F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain JM109 by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination, expression of the His-tagged enzyme in Escherichia coli strain JM109
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reger, A.S.; Wu, R.; Dunaway-Mariano, D.; Gulick, A.M.
Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase
Biochemistry
47
8016-8025
2008
Alcaligenes sp. (Q8GN86)
Manually annotated by BRENDA team
Wu, R.; Cao, J.; Lu, X.; Reger, A.S.; Gulick, A.M.; Dunaway-Mariano, D.
Mechanism of 4-chlorobenzoate:coenzyme A ligase catalysis
Biochemistry
47
8026-8039
2008
Alcaligenes sp. (Q8GN86)
Manually annotated by BRENDA team