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Information on EC 3.1.2.32 - 2-aminobenzoylacetyl-CoA thioesterase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC3.1.2.32
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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.32 2-aminobenzoylacetyl-CoA thioesterase
IUBMB Comments
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the production of the signal molecule 2-heptyl-4(1H)-quinolone (HHQ).
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This record set is specific for:
Pseudomonas aeruginosa
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
pa1000, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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).
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
-
-
0
?
cysteamine S-phosphate + H2O
cysteamine + phosphate
show the reaction diagram
-
-
0
?
S-(4-nitrobenzoyl)mercaptoethane + H2O
4-nitrobenzoate + mercaptoethane
show the reaction diagram
-
-
0
?
S-ethyl-acetothioacetate + H2O
3-oxobutanoic acid + thioethanol
show the reaction diagram
-
-
0
?
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
2-aminobenzoylacetyl-CoA + H2O
2-aminobenzoylacetate + CoA
show the reaction diagram
-
-
-
?
additional information
?
-
no substrates: anthraniloyl-CoA (or benzoyl-CoA), malonyl-CoA and octanoyl-CoA
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
9.7fold stimulation of EDTA-treated protein
Fe2+
3.3fold stimulation of EDTA-treated protein. Protein has a Fe(II)Fe(III) center in the active site, crystallization data
Mn2+
7.9fold stimulation of EDTA-treated protein
Ni2+
1.9fold stimulation of EDTA-treated protein
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(1H-pyrrol-1-yl)benzoic acid
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
compound binds to the active center, presence does not affect the levels of the PqsE-regulated virulence factor pyocyanin
2-aminobenzoylacetate
compound binds to the active center, presence does not affect the levels of the PqsE-regulated virulence factor pyocyanin
3-methylthiophene-2-carboxylic acid
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
pH 8.2, 30°C
0.8
cysteamine S-phosphate
pH 8.2, 30°C
0.013 - 0.014
S-(4-nitrobenzoyl)mercaptoethane
-
4.4
S-ethyl-acetothioacetate
pH 8.2, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36
acetoacetyl-CoA
pH 8.2, 30°C
0.022
cysteamine S-phosphate
pH 8.2, 30°C
0.003 - 0.12
S-(4-nitrobenzoyl)mercaptoethane
-
0.85
S-ethyl-acetothioacetate
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
pH 8.5, 21°C
0.025
2-(pyridin-3-yl)benzoic acid
Pseudomonas aeruginosa
pH 8.5, 21°C
0.04
3-methylthiophene-2-carboxylic acid
Pseudomonas aeruginosa
pH 8.5, 21°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D130A
mutant in KH-like motif, pyocyanin production 0.2 mg/l compared with 6.2 mg/l for wild-type
D178A
active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
D73A
active site mutant, pyocyanin production 4.1 mg/l compared with 6.2 mg/l for wild-type
E182A
F195A
active site mutant, pyocyanin production 0.8 mg/l compared with 6.2 mg/l for wild-type
F276A
active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
H159A
active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
H221A
active site mutant, pyocyanin production 1.1 mg/l compared with 6.2 mg/l for wild-type
H282A
C-terminal alpha-helix mutant, pyocyanin production 0.4 mg/l compared with 6.2 mg/l for wild-type
H69A
active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
H71A
active site mutant, pyocyanin production 2.7 mg/l compared with 6.2 mg/l for wild-type
H74A
active site mutant, pyocyanin production 3.5 mg/l compared with 6.2 mg/l for wild-type
K101A
mutant in KH-like motif, pyocyanin production 4.4 mg/l compared with 6.2 mg/l for wild-type
L193A
active site mutant, pyocyanin production 4.7 mg/l compared with 6.2 mg/l for wild-type
L248A
C-terminal alpha-helix mutant, pyocyanin production 4.1 mg/l compared with 6.2 mg/l for wild-type
L261A
C-terminal alpha-helix mutant, pyocyanin production 0.2 mg/l compared with 6.2 mg/l for wild-type
L277A
active site mutant, pyocyanin production 4.5 mg/l compared with 6.2 mg/l for wild-type
L290A
C-terminal alpha-helix mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
M286A
C-terminal alpha-helix mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
Q272A
active site mutant, pyocyanin production 1.4 mg/l compared with 6.2 mg/l for wild-type
R107A
mutant in KH-like motif, pyocyanin production 4.0 mg/l compared with 6.2 mg/l for wild-type
R111A
mutant in KH-like motif, pyocyanin production 0.3 mg/l compared with 6.2 mg/l for wild-type
R288A
active site mutant, pyocyanin production 5.2 mg/l compared with 6.2 mg/l for wild-type
R95A
mutant in KH-like motif, pyocyanin production 5.1 mg/l compared with 6.2 mg/l for wild-type
S273A
active site mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
S285A
active site mutant, pyocyanin production 5.0 mg/l compared with 6.2 mg/l for wild-type
S285W
active site mutant, pyocyanin production 5.6 mg/l compared with 6.2 mg/l for wild-type
W269A
C-terminal alpha-helix mutant, pyocyanin production 0.1 mg/l compared with 6.2 mg/l for wild-type
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zender, M.; Witzgall, F.; Drees, S.L.; Weidel, E.; Maurer, C.K.; Fetzner, S.; Blankenfeldt, W.; Empting, M.; Hartmann, R.W.
Dissecting the multiple roles of PqsE in Pseudomonas aeruginosa virulence by discovery of small tool compounds
ACS Chem. Biol.
11
1755-1763
2016
Pseudomonas aeruginosa (P20581), Pseudomonas aeruginosa DSM 22644 (P20581)
Manually annotated by BRENDA team
Yu, S.; Jensen, V.; Seeliger, J.; Feldmann, I.; Weber, S.; Schleicher, E.; Haeussler, S.; Blankenfeldt, W.
Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein
Biochemistry
48
10298-10307
2009
Pseudomonas aeruginosa (P20581), Pseudomonas aeruginosa DSM 22644 (P20581)
Manually annotated by BRENDA team
Drees, S.L.; Fetzner, S.
PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules
Chem. Biol.
22
611-618
2015
Pseudomonas aeruginosa (A0A0H2Z6F6), Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2Z6F6)
Manually annotated by BRENDA team
Folch, B.; Deziel, E.; Doucet, N.
Systematic mutational analysis of the putative hydrolase PqsE: toward a deeper molecular understanding of virulence acquisition in Pseudomonas aeruginosa
PLoS ONE
8
e73727
2013
Pseudomonas aeruginosa (A0A0H2Z6F6), Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2Z6F6)
Manually annotated by BRENDA team
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