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Information on EC 3.1.2.23 - 4-hydroxybenzoyl-CoA thioesterase and Organism(s) Pseudomonas sp. and UniProt Accession P56653

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.23 4-hydroxybenzoyl-CoA thioesterase
IUBMB Comments
This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
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This record set is specific for:
Pseudomonas sp.
UNIPROT: P56653
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The taxonomic range for the selected organisms is: Pseudomonas sp.
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-HBA-CoA thioesterase
-
4-hydroxybenzoyl coenzyme A thioesterase
-
4-HBA-CoA thioesterase
-
-
4-hydroxybenzoyl coenzyme A hydrolase
-
-
4-hydroxybenzoyl coenzyme A thioesterase
-
-
Hydrolase, 4-hydroxybenzoyl coenzyme A
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
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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-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
-
-
-
?
4-Chlorobenzoyl-CoA + H2O
4-Chlorobenzoate + CoA
show the reaction diagram
-
-
-
?
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
show the reaction diagram
4-Hydroxybenzoyl-CoA + H2O
?
show the reaction diagram
-
the enzyme is involved in the pathway by which this organism converts 4-chlorobenzoate to 4-hydroxybenzoate
-
-
?
Benzoyl-CoA + H2O
Benzoate + CoA
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
show the reaction diagram
4-Hydroxybenzoyl-CoA + H2O
?
show the reaction diagram
-
the enzyme is involved in the pathway by which this organism converts 4-chlorobenzoate to 4-hydroxybenzoate
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxybenzyl-CoA
-
-
4-hydroxyphenacyl-CoA
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
550
4-chlorobenzoyl-CoA
pH 7.5, 25°C
5 - 20
4-fluorobenzoyl-CoA
pH 7.5, 25°C
0.006
4-hydroxybenzoyl-CoA
pH 7.5, 25°C
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
510
benzoyl-CoA
pH 7.5, 25°C
0.19
4-chlorobenzoyl-CoA
-
-
0.00014 - 0.0073
4-hydroxybenzoyl-CoA
0.2
benzoyl-CoA
-
-
additional information
additional information
-
kinetics and thermodynamic of enzyme-ligand binding
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
4-chlorobenzoyl-CoA
pH 7.5, 25°C
9.7
4-fluorobenzoyl-CoA
pH 7.5, 25°C
18.3
4-hydroxybenzoyl-CoA
pH 7.5, 25°C
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
1
benzoyl-CoA
pH 7.5, 25°C
0.123
4-Chlorobenzoate
-
-
0.00055 - 6.8
4-hydroxybenzoyl-CoA
0.26
benzoyl-CoA
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011 - 0.004
4-hydroxyphenacyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
-
4 * 16000, SDS-PAGE
16107
-
4 * 16107, calculation from nucleotide sequence
66000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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., Arthrobacter sp. SU / DSM 20407, Pseudomonas sp., Pseudomonas sp. CBS-3
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team