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Enzyme Nomenclature
Information on EC 3.1.2.32 - 2-aminobenzoylacetyl-CoA thioesterase and Organism(s) Pseudomonas aeruginosa
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3.1.2.32 2-aminobenzoylacetyl-CoA thioesteraseIUBMB 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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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Pseudomonas aeruginosa
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
pqsE
pqsE
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cysteamine S-phosphate + H2O
cysteamine + phosphate
-
-
-
?
S-(4-nitrobenzoyl)mercaptoethane + H2O
4-nitrobenzoate + mercaptoethane
-
-
-
-
?
S-ethyl-acetothioacetate + H2O
3-oxobutanoic acid + thioethanol
-
-
-
?
2-aminobenzoylacetyl-CoA + H2O
2-aminobenzoylacetate + CoA
-
-
-
?
additional information
?
-
no substrates: anthraniloyl-CoA (or benzoyl-CoA), malonyl-CoA and octanoyl-CoA
-
-
-
additional information
?
-
-
the enzyme slowly hydrolyzes phosphodiesters including single- and double-strandedDNA as well as mRNA and also the thioester S-(4-nitrobenzoyl)mercaptoethane. No substrates: acetyl-CoA, malonyl-CoA, benzoyl-CoA, L-lactoylglutathione
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoylacetyl-CoA + H2O
2-aminobenzoylacetate + CoA
-
-
-
?
additional information
?
-
no substrates: anthraniloyl-CoA (or benzoyl-CoA), malonyl-CoA and octanoyl-CoA
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
3.3fold stimulation of EDTA-treated protein. Protein has a Fe(II)Fe(III) center in the active site, crystallization data
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
0.013
S-(4-nitrobenzoyl)mercaptoethane
-
mutant E182A, pH 8.5, 25°C, presence of Mn2+
-
0.014
S-(4-nitrobenzoyl)mercaptoethane
-
wild-type, pH 8.5, 25°C, presence of Mn2+
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
S-(4-nitrobenzoyl)mercaptoethane
-
mutant E182A, pH 8.5, 25°C, presence of Mn2+
-
0.12
S-(4-nitrobenzoyl)mercaptoethane
-
wild-type, pH 8.5, 25°C, presence of Mn2+
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
enzyme is part of the quinolone signal pathway. The regulatory function of PqsE is not linked to its thioesterase activity and must be encoded outside of the active center
physiological function
-
in biosynthesis of the alkylquinolones 2-heptyl-3-hydroxy-4(1H)-quinolone and 2-heptyl-4(1H)-quinolone, PqsE acts as thioesterase, hydrolyzing the biosynthetic intermediate 2-aminobenzoylacetyl-coenzyme A to form 2-aminobenzoylacetate, the precursor of 2-heptyl-4(1H)-quinolone and 2-aminoacetophenone. The role of PqsE can be taken over to some extent by the broad-specificity thioesterase TesB. A pqsE mutant produces increased levels of 2,4-dihydroxyquinoline, resulting from intramolecular cyclization of 2-aminobenzoylacetyl-coenzyme A
physiological function
-
the active site of the enzyme involves residues that extend further into the hydrophobic core of the protein, advocating for a lid-like movement of the two terminal helices. A unique C-terminal alpha-helical motif is important for the molecular 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
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
E182A
-
significant decrease in kcat value for S-(4-nitrobenzoyl)mercaptoethane
E182A
-
active site mutant, pyocyanin production 1.2 mg/l compared with 6.2 mg/l for wild-type
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
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)
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)
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)
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