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EC Tree
IUBMB Comments This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
4-hydroxybenzoyl-coa thioesterase, 4-hydroxybenzoyl-coenzyme a thioesterase, 4-hba-coa thioesterase,
more
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4-hydroxybenzoyl coenzyme A hydrolase
4-hydroxybenzoyl coenzyme A thioesterase
4-hydroxybenzoyl-coenzyme A thioesterase
benzoyl-coenzyme A thioesterase
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Hydrolase, 4-hydroxybenzoyl coenzyme A
4-HBA-CoA thioesterase
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4-HBA-CoA thioesterase
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4-HBA-CoA thioesterase
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4-HBA-CoA thioesterase
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4-hydroxybenzoyl coenzyme A hydrolase
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4-hydroxybenzoyl coenzyme A hydrolase
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4-hydroxybenzoyl coenzyme A thioesterase
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4-hydroxybenzoyl coenzyme A thioesterase
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4-hydroxybenzoyl coenzyme A thioesterase
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4-hydroxybenzoyl-coenzyme A thioesterase
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4-hydroxybenzoyl-coenzyme A thioesterase
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Hydrolase, 4-hydroxybenzoyl coenzyme A
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Hydrolase, 4-hydroxybenzoyl coenzyme A
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Hydrolase, 4-hydroxybenzoyl coenzyme A
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Hydrolase, 4-hydroxybenzoyl coenzyme A
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Hydrolase, 4-hydroxybenzoyl coenzyme A
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Hydrolase, 4-hydroxybenzoyl coenzyme A
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4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
mechanism
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4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
active site structure and ligand binding mechanism, overview
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4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
catalytic sites of wild-type and mutant enzymes, substrate binding modifications, reaction kinetics
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4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
substrate and inhibitor binding by wild-type and mutant D17N enzymes, reaction mechanism and active site structure
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4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
catalytic sites of wild-type and mutant enzymes, substrate binding modifications, reaction kinetics
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4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
active site structure and ligand binding mechanism, overview
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4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
mechanism
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4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
substrate and inhibitor binding by wild-type and mutant D17N enzymes, reaction mechanism and active site structure
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4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
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hydrolysis of thioester
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hydrolysis of thioester
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hydrolysis of thioester
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hydrolysis of thioester
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hydrolysis of thioester
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hydrolysis of thioester
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hydrolysis of thioester
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4-hydroxybenzoyl-CoA hydrolase
This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O
2,3-dihydro-2,3-dihydroxybenzoate + CoA
-
-
-
?
2-aminobenzoyl-CoA + H2O
2-aminobenzoate + CoA
305% relative activity with 2-aminobenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-fluorobenzoyl-CoA + H2O
2-fluorobenzoate + CoA
189% relative activity with 2-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-hydroxybenzoyl-CoA + H2O
2-hydroxybenzoate + CoA
486% relative activity with 2-hydroxybenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-methylbenzoyl-CoA + H2O
2-methylbenzoate + CoA
10% relative activity with 2-methylbenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
4-Chlorobenzoyl-CoA + H2O
4-Chlorobenzoate + CoA
4-fluorobenzoyl-CoA + H2O
4-fluorobenzoate + CoA
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
4-Hydroxybenzoyl-CoA + H2O
?
4-methoxybenzoyl-CoA + H2O
4-methoxybenzoate + CoA
-
-
-
?
4-methylbenzoyl-CoA + H2O
4-methylbenzoate + CoA
-
-
-
?
4-trifluoromethylbenzoyl-CoA + H2O
4-trifluoromethylbenzoate + CoA
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-
-
?
Benzoyl-CoA + H2O
Benzoate + CoA
additional information
?
-
4-Chlorobenzoyl-CoA + H2O
4-Chlorobenzoate + CoA
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-
-
?
4-Chlorobenzoyl-CoA + H2O
4-Chlorobenzoate + CoA
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-
-
?
4-Chlorobenzoyl-CoA + H2O
4-Chlorobenzoate + CoA
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-
-
?
4-fluorobenzoyl-CoA + H2O
4-fluorobenzoate + CoA
380% relative activity with 4-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
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-
?
4-fluorobenzoyl-CoA + H2O
4-fluorobenzoate + CoA
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-
-
?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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-
-
?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
1300% relative activity with 4-hydroxybenzoyl-CoA compared to benzoyl-CoA as substrate
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-
?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
-
-
-
-
?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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-
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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-
?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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enzyme is part of the dehalogenation pathway of 4-chlorobenzoyl-CoA in soil bacteria
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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the CoA pantothenic acid moiety is inserted into the outer part of the active site tunnel and the nucleotide moiety is anchored to the protein surface, whereas the hydroxybenzoyl group binds in an enclosed pocket. Product 4-hydroxybenzoate is released from the active site of the enzyme prior to the release of product CoA following catalytic turnover. 4-Hydroxybenzoate dissociates directly from the hydroxybenzoyl binding pocket more quickly than CoA can move out of the connecting tunnel
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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enzyme is part of the dehalogenation pathway of 4-chlorobenzoyl-CoA in soil bacteria
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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the CoA pantothenic acid moiety is inserted into the outer part of the active site tunnel and the nucleotide moiety is anchored to the protein surface, whereas the hydroxybenzoyl group binds in an enclosed pocket. Product 4-hydroxybenzoate is released from the active site of the enzyme prior to the release of product CoA following catalytic turnover. 4-Hydroxybenzoate dissociates directly from the hydroxybenzoyl binding pocket more quickly than CoA can move out of the connecting tunnel
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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enzyme is part of the dehalogenation pathway of 4-chlorobenzoyl-CoA in soil bacteria
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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enzyme is part of the dehalogenation pathway of 4-chlorobenzoyl-CoA in soil bacteria
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
?
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the enzyme is involved in the pathway by which this organism converts 4-chlorobenzoate to 4-hydroxybenzoate
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?
4-Hydroxybenzoyl-CoA + H2O
?
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the enzyme is involved in the pathway by which this organism converts 4-chlorobenzoate to 4-hydroxybenzoate
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?
Benzoyl-CoA + H2O
Benzoate + CoA
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?
Benzoyl-CoA + H2O
Benzoate + CoA
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?
Benzoyl-CoA + H2O
Benzoate + CoA
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?
Benzoyl-CoA + H2O
Benzoate + CoA
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?
additional information
?
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the intermediates of the pathway are processed as coenzyme A thioesters and the cleavage of the aromatic ring is non-xygenolytic
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?
additional information
?
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the intermediates of the pathway are processed as coenzyme A thioesters and the cleavage of the aromatic ring is non-xygenolytic
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?
additional information
?
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residue Glu73 functions in nucleophilic catalysis, Gly65 and Gln58 contribute to transition-state stabilization via hydrogen bond formation with the thioester moiety and Thr77 orients the water nucleophile for attack at the 4-hydroxybenzoyl carbon of the enzymeanhydride intermediate. Mutation E73D switches the function of the carboxylate residue from nucleophilic catalysis to base catalysis and thus, the reaction from a two-step process involving a covalent enzyme intermediate to a single-step hydrolysis reaction. The substrate nucleotide unit is bound to the enzyme surface
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?
additional information
?
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residue Glu73 functions in nucleophilic catalysis, Gly65 and Gln58 contribute to transition-state stabilization via hydrogen bond formation with the thioester moiety and Thr77 orients the water nucleophile for attack at the 4-hydroxybenzoyl carbon of the enzymeanhydride intermediate. Mutation E73D switches the function of the carboxylate residue from nucleophilic catalysis to base catalysis and thus, the reaction from a two-step process involving a covalent enzyme intermediate to a single-step hydrolysis reaction. The substrate nucleotide unit is bound to the enzyme surface
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?
additional information
?
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residue Glu73 functions in nucleophilic catalysis, Gly65 and Gln58 contribute to transition-state stabilization via hydrogen bond formation with the thioester moiety and Thr77 orients the water nucleophile for attack at the 4-hydroxybenzoyl carbon of the enzymeanhydride intermediate. Mutation E73D switches the function of the carboxylate residue from nucleophilic catalysis to base catalysis and thus, the reaction from a two-step process involving a covalent enzyme intermediate to a single-step hydrolysis reaction. The substrate nucleotide unit is bound to the enzyme surface
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?
additional information
?
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reaction proceeds via formation of an aspartyl17-(4-hydroxybenzoyl)anhydride intermediate that undergoes rate-limiting hydrolytic cleavage at the hydroxybenzoyl carbonyl carbon atom. CoA and 4-hydroxybenzoate binding is weak
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?
additional information
?
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reaction proceeds via formation of an aspartyl17-(4-hydroxybenzoyl)anhydride intermediate that undergoes rate-limiting hydrolytic cleavage at the hydroxybenzoyl carbonyl carbon atom. CoA and 4-hydroxybenzoate binding is weak
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?
additional information
?
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reaction proceeds via formation of an aspartyl17-(4-hydroxybenzoyl)anhydride intermediate that undergoes rate-limiting hydrolytic cleavage at the hydroxybenzoyl carbonyl carbon atom. CoA and 4-hydroxybenzoate binding is weak
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-
?
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2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O
2,3-dihydro-2,3-dihydroxybenzoate + CoA
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-
-
?
2-aminobenzoyl-CoA + H2O
2-aminobenzoate + CoA
305% relative activity with 2-aminobenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-fluorobenzoyl-CoA + H2O
2-fluorobenzoate + CoA
189% relative activity with 2-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-hydroxybenzoyl-CoA + H2O
2-hydroxybenzoate + CoA
486% relative activity with 2-hydroxybenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-methylbenzoyl-CoA + H2O
2-methylbenzoate + CoA
10% relative activity with 2-methylbenzoyl-CoA compared to benzoyl-CoA as substrate
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-
?
4-fluorobenzoyl-CoA + H2O
4-fluorobenzoate + CoA
380% relative activity with 4-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
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-
?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
4-Hydroxybenzoyl-CoA + H2O
?
Benzoyl-CoA + H2O
Benzoate + CoA
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-
-
?
additional information
?
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4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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-
-
?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
1300% relative activity with 4-hydroxybenzoyl-CoA compared to benzoyl-CoA as substrate
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
-
enzyme is part of the dehalogenation pathway of 4-chlorobenzoyl-CoA in soil bacteria
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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enzyme is part of the dehalogenation pathway of 4-chlorobenzoyl-CoA in soil bacteria
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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enzyme is part of the dehalogenation pathway of 4-chlorobenzoyl-CoA in soil bacteria
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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enzyme is part of the dehalogenation pathway of 4-chlorobenzoyl-CoA in soil bacteria
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?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
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?
4-Hydroxybenzoyl-CoA + H2O
?
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the enzyme is involved in the pathway by which this organism converts 4-chlorobenzoate to 4-hydroxybenzoate
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?
4-Hydroxybenzoyl-CoA + H2O
?
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the enzyme is involved in the pathway by which this organism converts 4-chlorobenzoate to 4-hydroxybenzoate
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?
additional information
?
-
the intermediates of the pathway are processed as coenzyme A thioesters and the cleavage of the aromatic ring is non-xygenolytic
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?
additional information
?
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the intermediates of the pathway are processed as coenzyme A thioesters and the cleavage of the aromatic ring is non-xygenolytic
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-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
K+
recombinant enzyme tolerates up to 0.6 M KCl, 27% activity enhancement when 0.1 M KCl is added to the assay
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2,5-dihydroxybenzoyl-CoA
the strongest inhibitor of the di-substituted non-substrates
acetyl-CoA
inhibits the hydrolysis of benzoyl-CoA
phenylacetyl-CoA
inhibits the hydrolysis of benzoyl-CoA
4-hydroxybenzyl-CoA
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4-hydroxyphenacyl-CoA
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binding mechanism
4-hydroxyphenacyl-CoA
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additional information
di-substituted derivatives of benzoyl-CoA, phenylacetyl-CoA and aliphatic CoA thioesters are not hydrolyzed but some act as inhibitors
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additional information
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di-substituted derivatives of benzoyl-CoA, phenylacetyl-CoA and aliphatic CoA thioesters are not hydrolyzed but some act as inhibitors
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Gangliosidosis, GM1
Murine ?-galactosidase stability is not dependent on temperature or protective protein/cathepsin A.
Mucopolysaccharidosis IV
Murine ?-galactosidase stability is not dependent on temperature or protective protein/cathepsin A.
Neurodegenerative Diseases
Murine ?-galactosidase stability is not dependent on temperature or protective protein/cathepsin A.
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0.19 - 550
4-chlorobenzoyl-CoA
5 - 20
4-fluorobenzoyl-CoA
pH 7.5, 25°C
0.00014 - 0.51
4-hydroxybenzoyl-CoA
56
4-methoxybenzoyl-CoA
pH 7.5, 25°C
230
4-methylbenzoyl-CoA
pH 7.5, 25°C
300
4-trifluoromethylbenzoyl-CoA
pH 7.5, 25°C
additional information
additional information
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0.19
4-chlorobenzoyl-CoA
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550
4-chlorobenzoyl-CoA
pH 7.5, 25°C
0.00014
4-hydroxybenzoyl-CoA
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mutant K90A, pH 7.5, 25°C
0.00038
4-hydroxybenzoyl-CoA
mutant T77D, pH 7.5, 25°C
0.00077
4-hydroxybenzoyl-CoA
mutant T77S, pH 7.5, 25°C
0.0012
4-hydroxybenzoyl-CoA
wild-type, pH 7.5, 25°C
0.0012
4-hydroxybenzoyl-CoA
mutant T77A, pH 7.5, 25°C
0.0016
4-hydroxybenzoyl-CoA
mutant Q58A, pH 7.5, 25°C
0.0016
4-hydroxybenzoyl-CoA
mutant S120A, pH 7.5, 25°C
0.0024
4-hydroxybenzoyl-CoA
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mutant D17E, pH 7.5, 25°C
0.004
4-hydroxybenzoyl-CoA
mutant D31A, pH 7.5, 25°C
0.004
4-hydroxybenzoyl-CoA
mutant Q58E, pH 7.5, 25°C
0.0045
4-hydroxybenzoyl-CoA
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-
0.0045
4-hydroxybenzoyl-CoA
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mutant R88A, pH 7.5, 25°C
0.0046
4-hydroxybenzoyl-CoA
mutant E73D/T77A, pH 7.5, 25°C
0.005
4-hydroxybenzoyl-CoA
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mutant R126L, pH 7.5, 25°C
0.0052
4-hydroxybenzoyl-CoA
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mutant R89L, pH 7.5, 25°C
0.0055
4-hydroxybenzoyl-CoA
mutant T77V, pH 7.5, 25°C
0.006
4-hydroxybenzoyl-CoA
pH 7.5, 25°C
0.006
4-hydroxybenzoyl-CoA
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wild-type enzyme, pH 7.5, 25°C
0.0061
4-hydroxybenzoyl-CoA
mutant T121A, pH 7.5, 25°C
0.007
4-hydroxybenzoyl-CoA
recombinant enzyme
0.0073
4-hydroxybenzoyl-CoA
-
mutant R128A, pH 7.5, 25°C
0.0128
4-hydroxybenzoyl-CoA
mutant D31N, pH 7.5, 25°C
0.013
4-hydroxybenzoyl-CoA
mutant E73D/T77S, pH 7.5, 25°C
0.014
4-hydroxybenzoyl-CoA
mutant R102A, pH 7.5, 25°C
0.0142
4-hydroxybenzoyl-CoA
mutant E73Q, pH 7.5, 25°C
0.015
4-hydroxybenzoyl-CoA
mutant R150A, pH 7.5, 25°C
0.018
4-hydroxybenzoyl-CoA
mutant E73D, pH 7.5, 25°C
0.096
4-hydroxybenzoyl-CoA
mutant E78A, pH 7.5, 25°C
0.18
4-hydroxybenzoyl-CoA
mutant Q58D, pH 7.5, 25°C
0.237
4-hydroxybenzoyl-CoA
mutant H64Q, pH 7.5, 25°C
0.51
4-hydroxybenzoyl-CoA
mutant H64A, pH 7.5, 25°C
0.077
benzoyl-CoA
recombinant enzyme
510
benzoyl-CoA
pH 7.5, 25°C
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics and thermodynamic of enzyme-ligand binding
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.123
4-Chlorobenzoate
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-
1.1
4-chlorobenzoyl-CoA
pH 7.5, 25°C
9.7
4-fluorobenzoyl-CoA
pH 7.5, 25°C
0.0001 - 99
4-hydroxybenzoyl-CoA
0.27
4-methoxybenzoyl-CoA
pH 7.5, 25°C
0.047
4-methylbenzoyl-CoA
pH 7.5, 25°C
0.038
4-trifluoromethylbenzoyl-CoA
pH 7.5, 25°C
0.0001
4-hydroxybenzoyl-CoA
mutant E73A, pH 7.5, 25°C
0.00055
4-hydroxybenzoyl-CoA
-
mutant D17N, pH 7.5, 25°C
0.00084
4-hydroxybenzoyl-CoA
-
mutant D17S, pH 7.5, 25°C
0.0017
4-hydroxybenzoyl-CoA
mutant E73Q, pH 7.5, 25°C
0.0103
4-hydroxybenzoyl-CoA
mutant T77D, pH 7.5, 25°C
0.0417
4-hydroxybenzoyl-CoA
mutant D31A, pH 7.5, 25°C
0.11
4-hydroxybenzoyl-CoA
-
mutant R126L, pH 7.5, 25°C
0.123
4-hydroxybenzoyl-CoA
mutant E73D, pH 7.5, 25°C
0.127
4-hydroxybenzoyl-CoA
mutant Q58A, pH 7.5, 25°C
0.129
4-hydroxybenzoyl-CoA
mutant E73D/T77S, pH 7.5, 25°C
0.13
4-hydroxybenzoyl-CoA
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mutant R88A, pH 7.5, 25°C
0.13
4-hydroxybenzoyl-CoA
mutant Q58D, pH 7.5, 25°C
0.14
4-hydroxybenzoyl-CoA
-
mutant K90A, pH 7.5, 25°C
0.15
4-hydroxybenzoyl-CoA
-
mutant R128A, pH 7.5, 25°C
0.15
4-hydroxybenzoyl-CoA
mutant H64A, pH 7.5, 25°C
0.17
4-hydroxybenzoyl-CoA
mutant T77V, pH 7.5, 25°C
0.18
4-hydroxybenzoyl-CoA
-
wild-type enzyme and mutant R89L, pH 7.5, 25°C
0.28
4-hydroxybenzoyl-CoA
mutant H64Q, pH 7.5, 25°C
0.364
4-hydroxybenzoyl-CoA
mutant Q58E, pH 7.5, 25°C
0.48
4-hydroxybenzoyl-CoA
-
mutant D17E, pH 7.5, 25°C
1.08
4-hydroxybenzoyl-CoA
mutant E78A, pH 7.5, 25°C
1.15
4-hydroxybenzoyl-CoA
mutant D31N, pH 7.5, 25°C
1.54
4-hydroxybenzoyl-CoA
mutant E73D/T77A, pH 7.5, 25°C
2.09
4-hydroxybenzoyl-CoA
mutant T77A, pH 7.5, 25°C
2.4
4-hydroxybenzoyl-CoA
wild-type, solvent D2O, pH 7.5, 25°C
3.16
4-hydroxybenzoyl-CoA
mutant T77S, pH 7.5, 25°C
6.7
4-hydroxybenzoyl-CoA
wild-type, pH 7.5, 25°C
6.8
4-hydroxybenzoyl-CoA
-
-
9.5
4-hydroxybenzoyl-CoA
mutant R150A, pH 7.5, 25°C
9.7
4-hydroxybenzoyl-CoA
mutant T121A, pH 7.5, 25°C
10
4-hydroxybenzoyl-CoA
recombinant enzyme
10.1
4-hydroxybenzoyl-CoA
mutant S120A, pH 7.5, 25°C
18.3
4-hydroxybenzoyl-CoA
pH 7.5, 25°C
99
4-hydroxybenzoyl-CoA
mutant R102A, pH 7.5, 25°C
0.26
benzoyl-CoA
-
-
1
benzoyl-CoA
pH 7.5, 25°C
3
benzoyl-CoA
recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.12 - 6300
4-hydroxybenzoyl-CoA
0.12
4-hydroxybenzoyl-CoA
mutant E73Q, pH 7.5, 25°C
0.29
4-hydroxybenzoyl-CoA
mutant H64A, pH 7.5, 25°C
1.1
4-hydroxybenzoyl-CoA
mutant E78A, pH 7.5, 25°C
1.2
4-hydroxybenzoyl-CoA
mutant H64Q, pH 7.5, 25°C
6.8
4-hydroxybenzoyl-CoA
mutant E73D, pH 7.5, 25°C
10
4-hydroxybenzoyl-CoA
mutant D31A, pH 7.5, 25°C
10
4-hydroxybenzoyl-CoA
mutant E73D/T77S, pH 7.5, 25°C
27
4-hydroxybenzoyl-CoA
mutant T77D, pH 7.5, 25°C
31
4-hydroxybenzoyl-CoA
mutant T77V, pH 7.5, 25°C
72
4-hydroxybenzoyl-CoA
mutant Q58D, pH 7.5, 25°C
79
4-hydroxybenzoyl-CoA
mutant Q58A, pH 7.5, 25°C
90
4-hydroxybenzoyl-CoA
mutant D31N, pH 7.5, 25°C
91
4-hydroxybenzoyl-CoA
mutant Q58E, pH 7.5, 25°C
340
4-hydroxybenzoyl-CoA
mutant E73D/T77A, pH 7.5, 25°C
630
4-hydroxybenzoyl-CoA
mutant R150A, pH 7.5, 25°C
710
4-hydroxybenzoyl-CoA
mutant R102A, pH 7.5, 25°C
1600
4-hydroxybenzoyl-CoA
mutant T121A, pH 7.5, 25°C
1700
4-hydroxybenzoyl-CoA
mutant T77A, pH 7.5, 25°C
4100
4-hydroxybenzoyl-CoA
mutant T77S, pH 7.5, 25°C
5400
4-hydroxybenzoyl-CoA
wild-type, pH 7.5, 25°C
6300
4-hydroxybenzoyl-CoA
mutant S120A, pH 7.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0006
4-hydroxybenzyl-CoA
-
pH 7.5, 25°C
0.0000003 - 0.004
4-hydroxyphenacyl-CoA
0.0000003
4-hydroxyphenacyl-CoA
-
pH 7.5, 25°C
0.0011
4-hydroxyphenacyl-CoA
-
mutant R126L, pH 7.5, 25°C
0.0012
4-hydroxyphenacyl-CoA
-
mutant R88A, pH 7.5, 25°C
0.0014
4-hydroxyphenacyl-CoA
-
wild-type enzyme, pH 7.5, 25°C
0.0018
4-hydroxyphenacyl-CoA
-
mutant D17E, pH 7.5, 25°C
0.0021
4-hydroxyphenacyl-CoA
-
mutant R128A, pH 7.5, 25°C
0.004
4-hydroxyphenacyl-CoA
-
mutant K90A, pH 7.5, 25°C
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0.02
extract of cells grown aerobically on benzoate, hydrolysis of benzoyl-CoA
additional information
10% relative activity with 2-methylbenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
-
10% relative activity with 2-methylbenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
100% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate malonyl-CoA
additional information
-
100% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate malonyl-CoA
additional information
1300% relative activity with 4-hydroxybenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
-
1300% relative activity with 4-hydroxybenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
189% relative activity with 2-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
-
189% relative activity with 2-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
305% relative activity with 2-aminobenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
-
305% relative activity with 2-aminobenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
380% relative activity with 4-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
-
380% relative activity with 4-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
486% relative activity with 2-hydroxybenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
-
486% relative activity with 2-hydroxybenzoyl-CoA compared to benzoyl-CoA as substrate
additional information
56% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate phenylacetyl-CoA
additional information
-
56% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate phenylacetyl-CoA
additional information
70% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate 2,5-dihydroxybenzoyl-CoA
additional information
-
70% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate 2,5-dihydroxybenzoyl-CoA
additional information
76% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate acetyl-CoA
additional information
-
76% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate acetyl-CoA
additional information
80% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate 2,3-dihydroxybenzoyl-CoA
additional information
-
80% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate 2,3-dihydroxybenzoyl-CoA
additional information
90% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate 3,5-difluorobenzoyl-CoA
additional information
-
90% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate 3,5-difluorobenzoyl-CoA
additional information
90% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate 3,5-dihydroxybenzoyl-CoA
additional information
-
90% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate 3,5-dihydroxybenzoyl-CoA
additional information
90% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate DL-3-hydroxy-3-methylglutaryl-CoA
additional information
-
90% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate DL-3-hydroxy-3-methylglutaryl-CoA
additional information
90% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate DL-methylmalonyl-CoA
additional information
-
90% residual benzoyl-CoA thioesterase activity with benzoyl-CoA in the presence of the non-substrate DL-methylmalonyl-CoA
additional information
benzoyl-CoA thioesterase activity is specific for aerobic growth of Azoarcus evansii on benzoate
additional information
-
benzoyl-CoA thioesterase activity is specific for aerobic growth of Azoarcus evansii on benzoate
additional information
characterization is carried out using a 5,5-dithio-bis(2-nitrobenzoic acid)-based spectrophotometric assay performed at 30°C in 100 mM Tris-HCl buffer
additional information
-
characterization is carried out using a 5,5-dithio-bis(2-nitrobenzoic acid)-based spectrophotometric assay performed at 30°C in 100 mM Tris-HCl buffer
additional information
no benzoyl-CoA thioesterase activity can be detected in extracts of cells grown aerobically on phenylacetate and 3-hydroxybenzoate or grown anaerobically on benzoate, phenylacetate, 4-hydroxyphenylacetate and phenylalanine
additional information
-
no benzoyl-CoA thioesterase activity can be detected in extracts of cells grown aerobically on phenylacetate and 3-hydroxybenzoate or grown anaerobically on benzoate, phenylacetate, 4-hydroxyphenylacetate and phenylalanine
additional information
the enzyme exhibits higher activity with mono-substituted derivatives of benzoyl-CoA, showing highest activity with 4-hydroxybenzoyl-CoA
additional information
-
the enzyme exhibits higher activity with mono-substituted derivatives of benzoyl-CoA, showing highest activity with 4-hydroxybenzoyl-CoA
additional information
the recombinant enzyme catalyzes the hydrolysis of 4-hydroxybenzoyl-CoA with a Vmax of 48 micromol/min/mg protein
additional information
-
the recombinant enzyme catalyzes the hydrolysis of 4-hydroxybenzoyl-CoA with a Vmax of 48 micromol/min/mg protein
additional information
the recombinant enzyme catalyzes the hydrolysis of benzoyl-CoA with a Vmax of 13 micromol/min/mg protein
additional information
-
the recombinant enzyme catalyzes the hydrolysis of benzoyl-CoA with a Vmax of 13 micromol/min/mg protein
additional information
-
-
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10.5
recombinant enzyme shows half maximal activity
7.5
recombinant enzyme shows half maximal activity
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KB-740, DSMZ 6869, formerly designated Pseudomonas sp. KB740
UniProt
brenda
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brenda
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brenda
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UniProt
brenda
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brenda
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UniProt
brenda
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brenda
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SwissProt
brenda
CBS3, recombinantly expressed in Escherichia coli
SwissProt
brenda
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brenda
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SwissProt
brenda
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16107
-
4 * 16107, calculation from nucleotide sequence
62000
native protein, determined by gel filtration
16000
-
4 * 16000, SDS-PAGE
16000
4 * 16000, determined by gel filtration
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homotetramer
4 * 16000, determined by gel filtration
tetramer
-
dimer of dimers, structure analysis
tetramer
-
mass spectrometry
tetramer
-
dimer of dimers, structure analysis
-
tetramer
-
mass spectrometry
-
tetramer
-
4 * 16107, calculation from nucleotide sequence
tetramer
-
4 * 16000, SDS-PAGE
tetramer
-
4 * 16107, calculation from nucleotide sequence
-
tetramer
-
4 * 16000, SDS-PAGE
-
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purified recombinant wild-type enzyme with and without bound inhibitor, hanging drop vapour diffusion method, 4°C, 18 mg/ml protein solution containing 10 mM HEPES, pH 7.5, 150 mM KCl, 1 mM 1,4-dithio-D,L-threitol, with or without 1 mM 4-hydroxyphenacyl-CoA, plus precipitant solution containing 17-20% PEG 3400, 100 mM MOPS, pH 7.0, and 200 mM LiCl, X-ray diffraction structure determination at 2.6 A resolution, and analysis
-
wild-type and mutant structures in complex with ligands 4-hydroxybenzoyl-CoA or CoA
purified wild-type enzyme with bound inhibitors, 14 mg/ml protein solution containing 10 mM HEPES, pH 7.0, 200 mM KCl, 5 mM 4-hydroxyphenacyl-CoA or 4-hydroxybenzyl-CoA, addition of solution containing 10% polyethylene glycol 8000, 2% Me2SO4, 10 mM succinate, pH 5.0 at room temperature, larger crystals are obtained by usage of 2-45 PEG 8000, X-ray diffracion structure determination at 1.5-1.8 A and 4°C, and analysis, D17N mutant with bound substrate 4-hydroxybenzoyl-CoA, macro-seeding into batch technique, 5 mg/ml protein solution containing 8-10% PEG 5000-O-methyl ether, 200 mM KCl, 100 mM MES, pH 6.0, 1 mM substrate, room temperature, X-ray diffraction structure determination at 3.3 A and 4°C, and analysis
-
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D31A
steady-state kinetic analysis
D31N
steady-state kinetic analysis
E73A
steady-state kinetic analysis, crystallization data
E73D/T77A
mutant regains most of the catalytic efficiency lost in the E73D single mutant
E73D/T77S
steady-state kinetic analysis
E73Q
steady-state kinetic analysis, crystallization data
E78A
steady-state kinetic analysis
H64A
steady-state kinetic analysis, crystallization data
H64Q
steady-state kinetic analysis
Q58A
steady-state kinetic analysis, crystallization data
Q58D
steady-state kinetic analysis
Q58D/E73D NA
complete loss of activity
Q58E
steady-state kinetic analysis
Q58E/E73A NA
complete loss of activity
Q58E/E73Q NA
complete loss of activity
R102A
steady-state kinetic analysis
R150A
steady-state kinetic analysis
S120A
steady-state kinetic analysis
T121A
steady-state kinetic analysis
T77D
steady-state kinetic analysis
T77V
steady-state kinetic analysis
E73A
-
steady-state kinetic analysis, crystallization data
-
E78A
-
steady-state kinetic analysis
-
R102A
-
steady-state kinetic analysis
-
S120A
-
steady-state kinetic analysis
-
T77D
-
steady-state kinetic analysis
-
D17E
-
site-directed mutagensis, increased activity
D17S
-
site-directed mutagensis, highly reduced activity
K90A
-
site-directed mutagensis, enhanced sensitivity against inhibitor 4-hydroxyphenacyl-CoA
R126L
-
site-directed mutagensis, slightly reduced activity
R128A
-
site-directed mutagensis, similar to the wild-type enzyme
R88A
-
site-directed mutagensis, slightly reduced activity
R89L
-
site-directed mutagensis, similar to the wild-type enzyme
D17N
-
site-directed mutagensis, role of Asp17 in ligand binding
-
D17E
-
site-directed mutagensis, increased activity
-
D17N
-
site-directed mutagensis, highly reduced activity
-
D17S
-
site-directed mutagensis, highly reduced activity
-
K90A
-
site-directed mutagensis, enhanced sensitivity against inhibitor 4-hydroxyphenacyl-CoA
-
R88A
-
site-directed mutagensis, slightly reduced activity
-
E73D
mutation switches the function of the carboxylate residue from nucleophilic catalysis to base catalysis and thus, the reaction from a two-step process involving a covalent enzyme intermediate to a single-step hydrolysis reaction
E73D
steady-state kinetic analysis
T77A
configuration of the active site residues is unchanged. The Thr77 side chain is positioned to bind and orient a water molecule for attack at the benzoyl carbonyl carbon of the putative anhydride intermediate
T77A
steady-state kinetic analysis, crystallization data
T77S
Ser77 is more effective than is the Thr77 at positioning the water for attack at the 4-hydroxybenzoyl carbonyl carbon of the anhydride intermediate
T77S
steady-state kinetic analysis, crystallization data
D17N
-
site-directed mutagensis, highly reduced activity
D17N
-
site-directed mutagensis, role of Asp17 in ligand binding
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-20
recombinant enzyme retains activity without significant loss by keeping at -20°C for several months in Tris-HCl buffer at pH 8
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-20°C, recombinant enzyme, Tris-HCl buffer, pH 8, several months stable
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by nickel chelate affinity and gel filtration chromatography
-
-
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expression in Escherichia coli
-
the gene is cloned and overexpressed in Escherichia coli to produce a C-terminal His-tag fusion protein
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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. SU / DSM 20407, Pseudomonas sp. CBS-3
brenda
Benning, M.M.; Wesenberg, G.; Liu, R.; Taylor, K.L.; Duinaway-Mariano, D.; Holden, H.M.
The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. strain CBS-3
J. Biol. Chem.
273
33572-33579
1998
Pseudomonas sp., Pseudomonas sp. CBS-3
brenda
Zhuang, Z.; Song, F.; Zhang, W.; Taylor, K.; Archambault, A.; Dunaway-Mariano, D.; Dong, J.; Carey, P.R.
Kinetic, Raman, NMR, and site-directed mutagenesis studies of the Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase active site
Biochemistry
41
11152-11160
2002
Pseudomonas sp., Pseudomonas sp. CBS3
brenda
Thoden, J.B.; Holden, H.M.; Zhuang, Z.; Dunaway-Mariano, D.
X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase
J. Biol. Chem.
277
27468-27476
2002
Pseudomonas sp., Pseudomonas sp. CBS-3
brenda
Thoden, J.B.; Zhuang, Z.; Dunaway-Mariano, D.; Holden, H.M.
The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU
J. Biol. Chem.
278
43709-43716
2003
Arthrobacter sp., Arthrobacter sp. SU / DSM 20407
brenda
Song, F.; Zhuang, Z.; Dunaway-Mariano, D.
Structure-activity analysis of base and enzyme-catalyzed 4-hydroxybenzoyl coenzyme A hydrolysis
Bioorg. Chem.
35
1-10
2007
Pseudomonas sp. (P56653)
brenda
Ismail, W.
Benzoyl-coenzyme A thioesterase of Azoarcus evansii: properties and function
Arch. Microbiol.
190
451-460
2008
Aromatoleum evansii (Q84HI6), Aromatoleum evansii
brenda
Li, Z.; Song, F.; Zhuang, Z.; Dunaway-Mariano, D.; Anderson, K.S.
Monitoring enzyme catalysis in the multimeric state: direct observation of Arthrobacter 4-hydroxybenzoyl-coenzyme A thioesterase catalytic complexes using time-resolved electrospray ionization mass spectrometry
Anal. Biochem.
394
209-216
2009
Arthrobacter sp., Arthrobacter sp. SU / DSM 20407
brenda
Song, F.; Thoden, J.B.; Zhuang, Z.; Latham, J.; Trujillo, M.; Holden, H.M.; Dunaway-Mariano, D.
The catalytic mechanism of the hotdog-fold enzyme superfamily 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU
Biochemistry
51
7000-7016
2012
Arthrobacter sp. (Q04416), Arthrobacter sp., Arthrobacter sp. SU / DSM 20407 (Q04416)
brenda
Zhuang, Z.; Latham, J.; Song, F.; Zhang, W.; Trujillo, M.; Dunaway-Mariano, D.
Investigation of the catalytic mechanism of the hotdog-fold enzyme superfamily Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase
Biochemistry
51
786-794
2012
Pseudomonas sp. (P56653), Pseudomonas sp., Pseudomonas sp. CBS-3 (P56653)
brenda
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