Information on EC 3.1.2.32 - 2-aminobenzoylacetyl-CoA thioesterase

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The expected taxonomic range for this enzyme is: Pseudomonas aeruginosa

EC NUMBER
COMMENTARY hide
3.1.2.32
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RECOMMENDED NAME
GeneOntology No.
2-aminobenzoylacetyl-CoA thioesterase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-aminobenzoylacetyl-CoA + H2O = 2-aminobenzoylacetate + CoA
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-heptyl-3-hydroxy-4(1H)-quinolone biosynthesis
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Phenazine biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
2-aminobenzoylacetyl-CoA hydrolase
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the production of the signal molecule 2-heptyl-4(1H)-quinolone (HHQ).
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoylacetyl-CoA + H2O
2-aminobenzoylacetate + CoA
show the reaction diagram
acetoacetyl-CoA + H2O
3-oxobutanoic acid + CoA
show the reaction diagram
cysteamine S-phosphate + H2O
cysteamine + phosphate
show the reaction diagram
S-(4-nitrobenzoyl)mercaptoethane + H2O
4-nitrobenzoate + mercaptoethane
show the reaction diagram
S-ethyl-acetothioacetate + H2O
3-oxobutanoic acid + thioethanol
show the reaction diagram
additional information
?
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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-aminobenzoylacetyl-CoA + H2O
2-aminobenzoylacetate + CoA
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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9.7fold stimulation of EDTA-treated protein
Fe2+
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3.3fold stimulation of EDTA-treated protein. Protein has a Fe(II)Fe(III) center in the active site, crystallization data
Mn2+
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7.9fold stimulation of EDTA-treated protein
Ni2+
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1.9fold stimulation of EDTA-treated protein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(1H-pyrrol-1-yl)benzoic acid
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compound binds to the active center, presence does not affect the levels of the PqsE-regulated virulence factor pyocyanin
2-(pyridin-3-yl)benzoic acid
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compound binds to the active center, presence does not affect the levels of the PqsE-regulated virulence factor pyocyanin
2-aminobenzoylacetate
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compound binds to the active center, presence does not affect the levels of the PqsE-regulated virulence factor pyocyanin
3-methylthiophene-2-carboxylic acid
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compound binds to the active center, presence does not affect the levels of the PqsE-regulated virulence factor pyocyanin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
acetoacetyl-CoA
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pH 8.2, 30°C
0.8
cysteamine S-phosphate
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pH 8.2, 30°C
0.013 - 0.014
S-(4-nitrobenzoyl)mercaptoethane
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4.4
S-ethyl-acetothioacetate
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pH 8.2, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36
acetoacetyl-CoA
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pH 8.2, 30°C
0.022
cysteamine S-phosphate
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pH 8.2, 30°C
0.003 - 0.12
S-(4-nitrobenzoyl)mercaptoethane
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0.85
S-ethyl-acetothioacetate
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pH 8.2, 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.155
2-(1H-pyrrol-1-yl)benzoic acid
Pseudomonas aeruginosa;
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pH 8.5, 21°C
0.025
2-(pyridin-3-yl)benzoic acid
Pseudomonas aeruginosa;
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pH 8.5, 21°C
0.04
3-methylthiophene-2-carboxylic acid
Pseudomonas aeruginosa;
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pH 8.5, 21°C
PDB
SCOP
CATH
UNIPROT
ORGANISM
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with inhbitors 2-aminobenzoylacetate, 2-(pyridin-3-yl)benzoic acid, 2-(1H-pyrrol-1-yl)benzoic acid and 3-methylthiophene-2-carboxylic acid
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structure of recombinant PqsE. The Protein possesses a metallo-beta-lactamase fold with an Fe(II)Fe(III) center in the active site. A copurified ligand is benzoate
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D130A
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mutant in KH-like motif, pyocyanin production 0.2 mg/l compared with 6.2 mg/l for wild-type
D178A
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active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
D73A
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active site mutant, pyocyanin production 4.1 mg/l compared with 6.2 mg/l for wild-type
F195A
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active site mutant, pyocyanin production 0.8 mg/l compared with 6.2 mg/l for wild-type
F276A
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active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
H159A
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active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
H221A
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active site mutant, pyocyanin production 1.1 mg/l compared with 6.2 mg/l for wild-type
H282A
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C-terminal alpha-helix mutant, pyocyanin production 0.4 mg/l compared with 6.2 mg/l for wild-type
H69A
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active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
H71A
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active site mutant, pyocyanin production 2.7 mg/l compared with 6.2 mg/l for wild-type
H74A
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active site mutant, pyocyanin production 3.5 mg/l compared with 6.2 mg/l for wild-type
K101A
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mutant in KH-like motif, pyocyanin production 4.4 mg/l compared with 6.2 mg/l for wild-type
L193A
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active site mutant, pyocyanin production 4.7 mg/l compared with 6.2 mg/l for wild-type
L248A
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C-terminal alpha-helix mutant, pyocyanin production 4.1 mg/l compared with 6.2 mg/l for wild-type
L261A
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C-terminal alpha-helix mutant, pyocyanin production 0.2 mg/l compared with 6.2 mg/l for wild-type
L277A
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active site mutant, pyocyanin production 4.5 mg/l compared with 6.2 mg/l for wild-type
L290A
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C-terminal alpha-helix mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
M286A
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C-terminal alpha-helix mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
Q272A
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active site mutant, pyocyanin production 1.4 mg/l compared with 6.2 mg/l for wild-type
R107A
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mutant in KH-like motif, pyocyanin production 4.0 mg/l compared with 6.2 mg/l for wild-type
R111A
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mutant in KH-like motif, pyocyanin production 0.3 mg/l compared with 6.2 mg/l for wild-type
R288A
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active site mutant, pyocyanin production 5.2 mg/l compared with 6.2 mg/l for wild-type
R95A
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mutant in KH-like motif, pyocyanin production 5.1 mg/l compared with 6.2 mg/l for wild-type
S273A
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active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
S285A
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active site mutant, pyocyanin production 5.0 mg/l compared with 6.2 mg/l for wild-type
S285W
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active site mutant, pyocyanin production 5.6 mg/l compared with 6.2 mg/l for wild-type
W269A
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C-terminal alpha-helix mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
E182A
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significant decrease in kcat value for S-(4-nitrobenzoyl)mercaptoethane
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D130A
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mutant in KH-like motif, pyocyanin production 0.2 mg/l compared with 6.2 mg/l for wild-type
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H221A
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active site mutant, pyocyanin production 1.1 mg/l compared with 6.2 mg/l for wild-type
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H69A
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active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
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H74A
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active site mutant, pyocyanin production 3.5 mg/l compared with 6.2 mg/l for wild-type
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R288A
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active site mutant, pyocyanin production 5.2 mg/l compared with 6.2 mg/l for wild-type
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