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Information on EC 6.2.1.33 - 4-chlorobenzoate-CoA ligase
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EC Tree
6.2.1.33 4-chlorobenzoate-CoA ligaseIUBMB Comments
Requires Mg2+. This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
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Word Map
- 6.2.1.33
-
dehalogenase
- 4-hydroxybenzoate
-
thioesterase
- amp
-
half-reaction
-
thioester-forming
-
adenylate-forming
-
thioesterification
-
acyl-adenylate
- 4-hydroxybenzoyl-coa
-
homotetramer
-
dehalogenation
-
4-cba-coa
-
single-turnover
- pantetheine
- aryl-coa
- alcaligenes
-
diester
-
chlorinate
- mgatp
-
poised
-
arthrobacter
The enzyme appears in viruses and cellular organisms
Synonyms
4-chlorobenzoate:coa ligase, 4-chlorobenzoyl-coa ligase, 4-halobenzoate-coenzyme a ligase, 4-chlorobenzoate:coenzyme a ligase, 4-cba:coa ligase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-CB:CoA ligase
4-CBA:CoA ligase
-
-
-
-
4-Chlorobenzoate:coenzyme A ligase
4-Chlorobenzoyl-CoA ligase
-
-
-
-
4-Chlorobenzoyl-coenzyme A ligase
-
-
-
-
4-Halobenzoate-coenzyme A ligase
-
-
-
-
Synthetase, 4-chlorobenzoyl coenzyme A
-
-
-
-
4-Chlorobenzoate:coenzyme A ligase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
two-step reaction consisting of the adenylation of 4-chlorobenzoate with adenosine 5'-triphosphate followed by acyl transfer from 4-chlorobenzoyl adenosine 5'-monophosphate diester
-
4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
4-chlorobenzoyl-adenosine 5'-phosphate diester is formed by the first partial reaction
-
4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
kinetic reaction mechanism, overview
4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
the enzyme alternates between two conformations during catalysis of the two half-reactions, structure-function analysis, domain alternation strategy, overview
4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
two-step reaction consisting of the adenylation of 4-chlorobenzoate with adenosine 5'-triphosphate followed by acyl transfer from 4-chlorobenzoyl adenosine 5'-monophosphate diester
-
-
4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
4-chlorobenzoyl-adenosine 5'-phosphate diester is formed by the first partial reaction
-
-
4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
formation of thioester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
141583-20-2
-
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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
4-Chlorobenzoate + CoA + ADP
4-Chlorobenzoyl-CoA + AMP + phosphate
-
reaction with ADP at 7.5% of the reaction with ATP
-
-
?
4-Methoxybenzoate + CoA + ATP
4-Methoxybenzoyl-CoA + AMP + diphosphate
-
at 9% of the activity with 4-chlorobenzoate
-
-
?
4-Nitrobenzoate + CoA + ATP
4-Nitrobenzoyl-CoA + AMP + diphosphate
-
at 7% of the activity with 4-chlorobenzoate
-
-
?
ATP + 4-chlorobenzoate + CoA
AMP + diphosphate + 4-chlorobenzoyl-CoA
-
ATP in form of MgATP2-
-
-
?
4-Bromobenzoate + CoA + ATP
4-Bromobenzoyl-CoA + AMP + diphosphate
-
93% of the activity with 4-chlorobenzoate
-
-
?
4-Bromobenzoate + CoA + ATP
4-Bromobenzoyl-CoA + AMP + diphosphate
-
93% of the activity with 4-chlorobenzoate
-
-
?
4-Bromobenzoate + CoA + ATP
4-Bromobenzoyl-CoA + AMP + diphosphate
-
at 105% of the activity with 4-chlorobenzoate
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
the enzyme catalyzes the synthesis of 4-chlorobenzoyl-CoA, the first step in the 4-chlorobenzoate degradation pathway in 4-chlorobenzoate-degrading bacteria
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
the rate-limiting step in CBL catalysis follows the formation of 4-chlorobenzoate-CoA
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
-
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
-
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
-
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
4-chlorobenzoyl-adenosine 5'-phosphate diester is formed by the first partial reaction
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
negligible activity with UTP, CTP, and GTP
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
-
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
4-chlorobenzoyl-adenosine 5'-phosphate diester is formed by the first partial reaction
-
-
?
4-Chlorobenzoate + CoA + ATP
?
-
catalyzes the first step in the 4-chlorobenzoate degradation pathway
-
-
?
4-Chlorobenzoate + CoA + ATP
?
-
induced by growth with 4-chlorobenzoate as sole carbon source
-
-
?
4-Chlorobenzoate + CoA + ATP
?
-
catalyzes the first step in the 4-chlorobenzoate degradation pathway
-
-
?
4-Fluorobenzoate + CoA + ATP
4-Fluorobenzoyl-CoA + AMP + diphosphate
-
67% of the activity with 4-chlorobenzoate
-
-
?
4-Fluorobenzoate + CoA + ATP
4-Fluorobenzoyl-CoA + AMP + diphosphate
-
67% of the activity with 4-chlorobenzoate
-
-
?
4-Fluorobenzoate + CoA + ATP
4-Fluorobenzoyl-CoA + AMP + diphosphate
-
at 36% of the activity with 4-chlorobenzoate
-
-
?
4-Iodobenzoate + CoA + ATP
4-Iodobenzoyl-CoA + AMP + diphosphate
-
73% of the activity with 4-chlorobenzoate
-
-
?
4-Iodobenzoate + CoA + ATP
4-Iodobenzoyl-CoA + AMP + diphosphate
-
73% of the activity with 4-chlorobenzoate
-
-
?
4-Iodobenzoate + CoA + ATP
4-Iodobenzoyl-CoA + AMP + diphosphate
-
at 90% of the activity with 4-chlorobenzoate
-
-
?
4-Methylbenzoate + CoA + ATP
4-Methylbenzoyl-CoA + AMP + diphosphate
-
-
-
?
4-Methylbenzoate + CoA + ATP
4-Methylbenzoyl-CoA + AMP + diphosphate
-
at 22% of the activity with 4-chlorobenzoate
-
-
?
Benzoate + CoA + ATP
Benzoyl-CoA + AMP + diphosphate
-
62% of the activity with 4-chlorobenzoate
-
-
?
Benzoate + CoA + ATP
Benzoyl-CoA + AMP + diphosphate
-
at 5% of the activity with 4-chlorobenzoate
-
-
?
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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
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
-
-
?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
-
the enzyme catalyzes the synthesis of 4-chlorobenzoyl-CoA, the first step in the 4-chlorobenzoate degradation pathway in 4-chlorobenzoate-degrading bacteria
-
-
?
4-Chlorobenzoate + CoA + ATP
?
-
catalyzes the first step in the 4-chlorobenzoate degradation pathway
-
-
?
4-Chlorobenzoate + CoA + ATP
?
-
induced by growth with 4-chlorobenzoate as sole carbon source
-
-
?
4-Chlorobenzoate + CoA + ATP
?
-
catalyzes the first step in the 4-chlorobenzoate degradation pathway
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Mg2+
-
maximal initial rate of catalysis is achieved with an Mg2+:ATP ratio of 1:0.66 to 1:1.33
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP
is a noncompetitive inhibitor versus ATP and an uncompetitive versus CoA
4-chlorophenacyl-CoA
the product analogue traps the enzyme in the thioester-forming conformation, binding structure, overview
-
4-chlorophenacyl-CoA
a product analogue, noncompetitive versus 4-methylbenzoate and ATP, dead-end inhibitor
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
transient-state and steady-state kinetics of wild-type and mutant enzymes, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
additional information
additional information
inhibition kinetics, overview
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8 - 8.2
-
pH 5.8: about 50% of maximal activity, pH 8.2: about 80% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
-
10°C: about 80% of maximal activity, 40°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
Show AA Sequence and Transmembrane Helices (184 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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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
determination and analysis of the structure of CBL in the adenylate forming conformation bound to 4-chlorobenzoate and the adenylate-forming conformation bound to the adenylate intermediate, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, 1.0 and 2.2 A. Crystal structures of the enzyme both in the unliganded state and bound to 4-chlorobenzoate. The space group is P3(1)21 or P3(2)21 with a = b = 129.3 A, c = 71.5 A
-
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
mutant D402P, to 2.6 A resolution, and comparison with wild-type. The C-terminal domain rotates by about 140 degrees between the two states that catalyze the adenylation and thioester-forming half-reactions. The domain rotation is accompanied by a change in the main chain torsional angles of residue D402
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
D402P
crystallization data. Mutant adopts the proposed adenylate-forming conformation with very little change to the overall structure.The ability of the mutant to catalyze the adenylate-forming half-reaction is reduced by about 3fold, catalysis of the second half-reaction is reduced by 4 orders of magnitude
E306Q
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
G163I
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
G166I
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
K169M
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
P168A
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
E306Q
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
-
G163I
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
-
G166I
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
-
K169M
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
-
P168A
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain JM109 by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination, expression of the His-tagged enzyme in Escherichia coli strain JM109
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chang, K.H.; Xiang, H.; Dunaway-Mariano, D.
Acyl-adenylate motif of the acyl-adenylate/thioester-forming enzyme superfamily: a site-directed mutagenesis study with the Pseudomonas sp. strain CBS3 4-chlorobenzoate:coenzyme A ligase
Biochemistry
36
15650-15659
1997
Pseudomonas sp., Pseudomonas sp. CBS3
brenda
Chang, K.H.; Dunaway-Mariano, D.
Determination of the chemical pathway for 4-chlorobenzoate:coenzyme A ligase catalysis
Biochemistry
35
13478-13484
1996
Pseudomonas sp., Pseudomonas sp. CBS3
brenda
Loeffler, F.; Mueller, R.; Lingens, F.
Purification and properties of 4-halobenzoate-coenzyme A ligase from Pseudomonas sp. CBS3
Biol. Chem. Hoppe-Seyler
373
1001-1007
1992
Pseudomonas sp.
brenda
Loeffler, F.; Mueller, R.
Characterization of 4-chlorobenzoyl-coenzyme A ligase from the 4-chlorobenzoate degrading strain Pseudomonas sp. CBS3
DECHEMA Biotechnol. Conf. (Pt. A. Microbial Principles in Bioprocesses: Cell Culture Technology - Downstream Processing and Recovery)
5
25-28
1992
Pseudomonas sp.
-
brenda
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.
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
Pseudomonas sp.
brenda
Gulick, A.M.; Lu, X.; Dunaway-Mariano, D.
Crystal structure of 4-chlorobenzoate:CoA ligase/synthetase in the unliganded and aryl substrate-bound states
Biochemistry
43
8670-8679
2004
Alcaligenes sp.
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
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)
brenda
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)
brenda
Wu, R.; Reger, A.S.; Lu, X.; Gulick, A.M.; Dunaway-Mariano, D.
The mechanism of domain alternation in the acyl-adenylate forming ligase superfamily member 4-chlorobenzoate: coenzyme A ligase
Biochemistry
48
4115-4125
2009
Alcaligenes sp. AL3007, Alcaligenes sp. AL3007 (Q8GN86)
brenda
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