Information on EC 3.1.2.23 - 4-hydroxybenzoyl-CoA thioesterase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
3.1.2.23
-
RECOMMENDED NAME
GeneOntology No.
4-hydroxybenzoyl-CoA thioesterase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-Hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-chlorobenzoate degradation
-
-
4-hydroxybenzoate biosynthesis I (eukaryotes)
-
-
4-hydroxybenzoate biosynthesis V
-
-
Benzoate degradation
-
-
Biosynthesis of secondary metabolites
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Ubiquinone and other terpenoid-quinone biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxybenzoyl-CoA hydrolase
This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
141583-19-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
KB-740, DSMZ 6869, formerly designated Pseudomonas sp. KB740
UniProt
Manually annotated by BRENDA team
strain CBS3
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O
2,3-dihydro-2,3-dihydroxybenzoate + CoA
show the reaction diagram
-
-
-
?
2-aminobenzoyl-CoA + H2O
2-aminobenzoate + CoA
show the reaction diagram
305% relative activity with 2-aminobenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-fluorobenzoyl-CoA + H2O
2-fluorobenzoate + CoA
show the reaction diagram
189% relative activity with 2-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-hydroxybenzoyl-CoA + H2O
2-hydroxybenzoate + CoA
show the reaction diagram
486% relative activity with 2-hydroxybenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-methylbenzoyl-CoA + H2O
2-methylbenzoate + CoA
show the reaction diagram
10% relative activity with 2-methylbenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
4-Chlorobenzoyl-CoA + H2O
4-Chlorobenzoate + CoA
show the reaction diagram
4-fluorobenzoyl-CoA + H2O
4-fluorobenzoate + CoA
show the reaction diagram
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
show the reaction diagram
4-Hydroxybenzoyl-CoA + H2O
?
show the reaction diagram
4-methoxybenzoyl-CoA + H2O
4-methoxybenzoate + CoA
show the reaction diagram
-
-
-
?
4-methylbenzoyl-CoA + H2O
4-methylbenzoate + CoA
show the reaction diagram
-
-
-
?
4-trifluoromethylbenzoyl-CoA + H2O
4-trifluoromethylbenzoate + CoA
show the reaction diagram
-
-
-
?
Benzoyl-CoA + H2O
Benzoate + CoA
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O
2,3-dihydro-2,3-dihydroxybenzoate + CoA
show the reaction diagram
Q84HI6
-
-
-
?
2-aminobenzoyl-CoA + H2O
2-aminobenzoate + CoA
show the reaction diagram
Q84HI6
305% relative activity with 2-aminobenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-fluorobenzoyl-CoA + H2O
2-fluorobenzoate + CoA
show the reaction diagram
Q84HI6
189% relative activity with 2-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-hydroxybenzoyl-CoA + H2O
2-hydroxybenzoate + CoA
show the reaction diagram
Q84HI6
486% relative activity with 2-hydroxybenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
2-methylbenzoyl-CoA + H2O
2-methylbenzoate + CoA
show the reaction diagram
Q84HI6
10% relative activity with 2-methylbenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
4-fluorobenzoyl-CoA + H2O
4-fluorobenzoate + CoA
show the reaction diagram
Q84HI6
380% relative activity with 4-fluorobenzoyl-CoA compared to benzoyl-CoA as substrate
-
-
?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
show the reaction diagram
4-Hydroxybenzoyl-CoA + H2O
?
show the reaction diagram
Benzoyl-CoA + H2O
Benzoate + CoA
show the reaction diagram
Q84HI6
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
recombinant enzyme tolerates up to 0.6 M KCl, 27% activity enhancement when 0.1 M KCl is added to the assay
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,5-dihydroxybenzoyl-CoA
the strongest inhibitor of the di-substituted non-substrates
4-hydroxybenzyl-CoA
4-hydroxyphenacyl-CoA
acetyl-CoA
inhibits the hydrolysis of benzoyl-CoA
phenylacetyl-CoA
inhibits the hydrolysis of benzoyl-CoA
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 550
4-chlorobenzoyl-CoA
5 - 20
4-fluorobenzoyl-CoA
pH 7.5, 25C
0.00014 - 0.51
4-hydroxybenzoyl-CoA
56
4-methoxybenzoyl-CoA
pH 7.5, 25C
230
4-methylbenzoyl-CoA
pH 7.5, 25C
300
4-trifluoromethylbenzoyl-CoA
pH 7.5, 25C
0.077 - 510
benzoyl-CoA
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.123
4-Chlorobenzoate
Pseudomonas sp.
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-
1.1
4-chlorobenzoyl-CoA
Pseudomonas sp.
P56653
pH 7.5, 25C
9.7
4-fluorobenzoyl-CoA
Pseudomonas sp.
P56653
pH 7.5, 25C
0.0001 - 99
4-hydroxybenzoyl-CoA
0.27
4-methoxybenzoyl-CoA
Pseudomonas sp.
P56653
pH 7.5, 25C
0.047
4-methylbenzoyl-CoA
Pseudomonas sp.
P56653
pH 7.5, 25C
0.038
4-trifluoromethylbenzoyl-CoA
Pseudomonas sp.
P56653
pH 7.5, 25C
0.26 - 3
benzoyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 6300
4-hydroxybenzoyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
4-hydroxybenzyl-CoA
-
pH 7.5, 25C
0.0000003 - 0.004
4-hydroxyphenacyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
extract of cells grown aerobically on benzoate, hydrolysis of benzoyl-CoA
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
8.5
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
recombinant enzyme shows half maximal activity
10.5
recombinant enzyme shows half maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
native protein, determined by gel filtration
66000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 16000, determined by gel filtration
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type enzyme with and without bound inhibitor, hanging drop vapour diffusion method, 4C, 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
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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 4C, 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 4C, and analysis
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-20
recombinant enzyme retains activity without significant loss by keeping at -20C for several months in Tris-HCl buffer at pH 8
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, recombinant enzyme, Tris-HCl buffer, pH 8, several months stable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by nickel chelate affinity and gel filtration chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
the gene is cloned and overexpressed in Escherichia coli to produce a C-terminal His-tag fusion protein
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D31A
steady-state kinetic analysis
D31N
steady-state kinetic analysis
E73A
steady-state kinetic analysis, crystallization data
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; steady-state kinetic analysis
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
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; steady-state kinetic analysis, crystallization data
T77D
steady-state kinetic analysis
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; steady-state kinetic analysis, crystallization data
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
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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
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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
-
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