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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
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dehalogenase
- 4-hydroxybenzoate
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thioesterase
- amp
-
half-reaction
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thioester-forming
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adenylate-forming
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thioesterification
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acyl-adenylate
- 4-hydroxybenzoyl-coa
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homotetramer
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dehalogenation
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4-cba-coa
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single-turnover
- pantetheine
- aryl-coa
- alcaligenes
-
diester
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chlorinate
- mgatp
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poised
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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
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4-Chlorobenzoate:coenzyme A ligase
4-Chlorobenzoyl-CoA ligase
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4-Chlorobenzoyl-coenzyme A ligase
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4-Halobenzoate-coenzyme A ligase
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Synthetase, 4-chlorobenzoyl coenzyme A
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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
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4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
4-chlorobenzoyl-adenosine 5'-phosphate diester is formed by the first partial reaction
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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
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4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
4-chlorobenzoyl-adenosine 5'-phosphate diester is formed by the first partial reaction
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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
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reaction with ADP at 7.5% of the reaction with ATP
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?
4-Methoxybenzoate + CoA + ATP
4-Methoxybenzoyl-CoA + AMP + diphosphate
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at 9% of the activity with 4-chlorobenzoate
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?
4-Nitrobenzoate + CoA + ATP
4-Nitrobenzoyl-CoA + AMP + diphosphate
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at 7% of the activity with 4-chlorobenzoate
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?
ATP + 4-chlorobenzoate + CoA
AMP + diphosphate + 4-chlorobenzoyl-CoA
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ATP in form of MgATP2-
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?
4-Bromobenzoate + CoA + ATP
4-Bromobenzoyl-CoA + AMP + diphosphate
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93% of the activity with 4-chlorobenzoate
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?
4-Bromobenzoate + CoA + ATP
4-Bromobenzoyl-CoA + AMP + diphosphate
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93% of the activity with 4-chlorobenzoate
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?
4-Bromobenzoate + CoA + ATP
4-Bromobenzoyl-CoA + AMP + diphosphate
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at 105% of the activity with 4-chlorobenzoate
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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the enzyme catalyzes the synthesis of 4-chlorobenzoyl-CoA, the first step in the 4-chlorobenzoate degradation pathway in 4-chlorobenzoate-degrading bacteria
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
the rate-limiting step in CBL catalysis follows the formation of 4-chlorobenzoate-CoA
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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4-chlorobenzoyl-adenosine 5'-phosphate diester is formed by the first partial reaction
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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negligible activity with UTP, CTP, and GTP
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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4-chlorobenzoyl-adenosine 5'-phosphate diester is formed by the first partial reaction
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?
4-Chlorobenzoate + CoA + ATP
?
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catalyzes the first step in the 4-chlorobenzoate degradation pathway
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?
4-Chlorobenzoate + CoA + ATP
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induced by growth with 4-chlorobenzoate as sole carbon source
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?
4-Chlorobenzoate + CoA + ATP
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catalyzes the first step in the 4-chlorobenzoate degradation pathway
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?
4-Fluorobenzoate + CoA + ATP
4-Fluorobenzoyl-CoA + AMP + diphosphate
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67% of the activity with 4-chlorobenzoate
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?
4-Fluorobenzoate + CoA + ATP
4-Fluorobenzoyl-CoA + AMP + diphosphate
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67% of the activity with 4-chlorobenzoate
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?
4-Fluorobenzoate + CoA + ATP
4-Fluorobenzoyl-CoA + AMP + diphosphate
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at 36% of the activity with 4-chlorobenzoate
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?
4-Iodobenzoate + CoA + ATP
4-Iodobenzoyl-CoA + AMP + diphosphate
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73% of the activity with 4-chlorobenzoate
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?
4-Iodobenzoate + CoA + ATP
4-Iodobenzoyl-CoA + AMP + diphosphate
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73% of the activity with 4-chlorobenzoate
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?
4-Iodobenzoate + CoA + ATP
4-Iodobenzoyl-CoA + AMP + diphosphate
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at 90% of the activity with 4-chlorobenzoate
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?
4-Methylbenzoate + CoA + ATP
4-Methylbenzoyl-CoA + AMP + diphosphate
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?
4-Methylbenzoate + CoA + ATP
4-Methylbenzoyl-CoA + AMP + diphosphate
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at 22% of the activity with 4-chlorobenzoate
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?
Benzoate + CoA + ATP
Benzoyl-CoA + AMP + diphosphate
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62% of the activity with 4-chlorobenzoate
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?
Benzoate + CoA + ATP
Benzoyl-CoA + AMP + diphosphate
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at 5% of the activity with 4-chlorobenzoate
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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
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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?
4-Chlorobenzoate + CoA + ATP
4-Chlorobenzoyl-CoA + AMP + diphosphate
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the enzyme catalyzes the synthesis of 4-chlorobenzoyl-CoA, the first step in the 4-chlorobenzoate degradation pathway in 4-chlorobenzoate-degrading bacteria
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?
4-Chlorobenzoate + CoA + ATP
?
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catalyzes the first step in the 4-chlorobenzoate degradation pathway
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?
4-Chlorobenzoate + CoA + ATP
?
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induced by growth with 4-chlorobenzoate as sole carbon source
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?
4-Chlorobenzoate + CoA + ATP
?
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catalyzes the first step in the 4-chlorobenzoate degradation pathway
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?
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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+
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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
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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
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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
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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
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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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