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Information on EC 2.3.1.230 - 2-heptyl-4(1H)-quinolone synthase
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2.3.1.230 2-heptyl-4(1H)-quinolone synthaseIUBMB Comments
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is a heterodimeric complex. The PqsC subunit acquires an octanoyl group from octanoyl-CoA and attaches it to an internal cysteine residue. Together with the PqsB subunit, the proteins catalyse the coupling of the octanoyl group with (2-aminobenzoyl)acetate, leading to decarboxylation and dehydration events that result in closure of the quinoline ring.
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Word Map
- 2.3.1.230
-
arachidonic
-
20-hydroxyeicosatetraenoic
-
omega-hydroxylase
-
constrictor
- phenylephrine
-
microcirculation
- cyp4a2
- clofibrate
-
ppars
-
lauric
-
omega-hydroxylation
-
interlobar
-
20-hydroxyeicosa-6z,15z-dienoic
-
myogenic
- n-methylsulfonyl-12,12-dibromododec-11-enamide
-
proliferators
-
nafenopin
-
arterioles
-
vasoconstrictor
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
2-heptyl-4(1h)-quinolone synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PqsBC
PqsD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-(2-aminophenyl)decane-1,3-dione = 2-heptyl-4-quinolone + H2O
(1c)
-
-
-
octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O
overall reaction
-
-
-
octanoyl-CoA + L-cysteinyl-[PqsC protein] = S-octanoyl-L-cysteinyl-[PqsC protein] + CoA
(1a)
-
-
-
S-octanoyl-L-cysteinyl-[PqsC protein] + (2-aminobenzoyl)acetate = 1-(2-aminophenyl)decane-1,3-dione + CO2 + L-cysteinyl-[PqsC protein]
(1b)
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
octanoyl-CoA:2-aminobenzoylacetate octanoyltransferase
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is a heterodimeric complex. The PqsC subunit acquires an octanoyl group from octanoyl-CoA and attaches it to an internal cysteine residue. Together with the PqsB subunit, the proteins catalyse the coupling of the octanoyl group with (2-aminobenzoyl)acetate, leading to decarboxylation and dehydration events that result in closure of the quinoline ring.
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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
3-oxodecanoate + 2-aminobenzoyl-CoA
CoA + 2-heptyl-4(1H)-quinolone + CO2 + H2O
-
-
-
-
?
3-oxodecanoate + 2-aminobenzoyl-CoA
CoA + 2-heptyl-4-hydroxyquinoline + CO2 + H2O
-
-
-
-
?
3-oxodecanoyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 2-heptyl-3-hydroxy-4(1H)-quinolone + CO2
-
high concentrations and a longer incubation time is required in comparison to the free 3-oxodecanoic acid
-
-
?
3-oxodecanoyl-N-acetylcysteamine + 2-aminobenzoyl-CoA
N-acetylcysteamine + 2-heptyl-3-hydroxy-4(1H)-quinolone + CO2
-
high concentrations and a longer incubation time is required in comparison to the free 3-oxodecanoic acid
-
-
?
3-oxohexanoate + 2-aminobenzoyl-CoA
CoA + 2-propyl-4(1H)-quinolone + CO2 + H2O
-
-
-
-
?
3-oxopentanoate + 2-aminobenzoyl-CoA
CoA + 2-ethyl-4(1H)-quinolone + CO2 + H2O
-
-
-
-
?
malonyl-[acyl-carrier protein] + 2-aminobenzoyl-CoA
CoA + acyl-carrier protein + 4-hydroxy-2(1H)-quinolone + CO2
-
first, the 2-aminobenzoyl moiety is transferred to the active-site Cys of PqsD to form a 2-aminobenzoyl-PqsD intermediate, which then condenses with either malonyl-CoA or malonyl-acyl carrier protein to produce 3-(2-aminophenyl)-3-oxopropanoyl-CoA. This short-lived intermediate undergoes an intramolecular rearrangement to form 2,4-dihydroxyquinoline
i.e. 2,4-dihydroxyquinoline
-
?
additional information
?
-
-
no activity with malonic acid or 2-hydroxybenzoate
-
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
2-aminobenzoyl-CoA i.e. anthraniloyl-CoA
i.e. 2,4-dihydroxyquinoline
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
2-aminobenzoyl-CoA i.e. anthraniloyl-CoA
i.e. 2,4-dihydroxyquinoline
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
2-aminobenzoyl-CoA i.e. anthraniloyl-CoA. PqsD is a key enzyme in the biosynthesis of the signal molecules 2-heptyl-4-hydroxyquinoline and 4-hydroxy-2(1H)-quinolone, that are involved in regulation of virulence factor production and biofilm formation
i.e. 2,4-dihydroxyquinoline
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
2-aminobenzoyl-CoA i.e. anthraniloyl-CoA. The enzyme is involved in the biosynthesis of the Pseudomonas Quinolone Signal
i.e. 2,4-dihydroxyquinoline
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
the enzyme is involved in the biosynthesis of 2,4-dihydroxyquinoline. Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen that is a highly interactive organism secreting a variety of chemical signals. One intercellular signaling system unique to Pseudomonas and Burkholderia species is the production of hydrophobic quinolines. These quinoline derivatives are 4-hydroxy-2-heptylquinoline, 3,4-dihydroxy-2-heptylquinoline, and 2,4-dihydroxyquinoline
i.e. 2,4-dihydroxyquinoline
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
the enzyme is involved in the biosynthesis of the signal molecules 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone. These compounds are part of the quorum-sensing systems that is based on the production and release of small signaling molecules, called autoinducers, that increase in concentration as a function of cell density and activate corresponding transcriptional regulators after a threshold concentration has been reached
-
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
2-aminobenzoyl-CoA i.e. anthraniloyl-CoA. Ping-pong mechanism for PqsD with 2-aminobenzoyl-CoA as first substrate. Trajectory analysis of different PqsD complexes evidences ligand-dependent induced-fit motions affecting the modified 2-aminobenzoyl-CoA funnel access to the exposure of a secondary channel. A tunnel-network is formed in which Ser317 plays an important role by binding to both substrates
i.e. 2,4-dihydroxyquinoline
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
catalyzes the decarboxylative Claisen condensation with malonyl-CoA.
-
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
first, the 2-aminobenzoyl moiety is transferred to the active-site Cys of PqsD to form a 2-aminobenzoyl-PqsD intermediate, which then condenses with either malonyl-CoA or malonyl-acyl carrier protein to produce 3-(2-aminophenyl)-3-oxopropanoyl-CoA. This short-lived intermediate undergoes an intramolecular rearrangement to form 2,4-dihydroxyquinoline
i.e. 2,4-dihydroxyquinoline
-
?
octanoyl-CoA + (2-aminobenzoyl)acetate
2-heptyl-4-quinolone + CoA + CO2 + H2O
Q9I4X2; Q9I4X1
-
-
-
?
octanoyl-CoA + (2-aminobenzoyl)acetate
2-heptyl-4-quinolone + CoA + CO2 + H2O
Q9I4X2; Q9I4X1
-
-
-
?
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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
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
2-aminobenzoyl-CoA i.e. anthraniloyl-CoA
i.e. 2,4-dihydroxyquinoline
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
2-aminobenzoyl-CoA i.e. anthraniloyl-CoA. PqsD is a key enzyme in the biosynthesis of the signal molecules 2-heptyl-4-hydroxyquinoline and 4-hydroxy-2(1H)-quinolone, that are involved in regulation of virulence factor production and biofilm formation
i.e. 2,4-dihydroxyquinoline
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
2-aminobenzoyl-CoA i.e. anthraniloyl-CoA. The enzyme is involved in the biosynthesis of the Pseudomonas Quinolone Signal
i.e. 2,4-dihydroxyquinoline
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
the enzyme is involved in the biosynthesis of 2,4-dihydroxyquinoline. Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen that is a highly interactive organism secreting a variety of chemical signals. One intercellular signaling system unique to Pseudomonas and Burkholderia species is the production of hydrophobic quinolines. These quinoline derivatives are 4-hydroxy-2-heptylquinoline, 3,4-dihydroxy-2-heptylquinoline, and 2,4-dihydroxyquinoline
i.e. 2,4-dihydroxyquinoline
-
?
malonyl-CoA + 2-aminobenzoyl-CoA
2 CoA + 4-hydroxy-2(1H)-quinolone + CO2
-
the enzyme is involved in the biosynthesis of the signal molecules 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone. These compounds are part of the quorum-sensing systems that is based on the production and release of small signaling molecules, called autoinducers, that increase in concentration as a function of cell density and activate corresponding transcriptional regulators after a threshold concentration has been reached
-
-
?
octanoyl-CoA + (2-aminobenzoyl)acetate
2-heptyl-4-quinolone + CoA + CO2 + H2O
Q9I4X2; Q9I4X1
-
-
-
?
octanoyl-CoA + (2-aminobenzoyl)acetate
2-heptyl-4-quinolone + CoA + CO2 + H2O
Q9I4X2; Q9I4X1
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2-nitrophenyl)(thiophen-3-yl)methanol
inhibitor shows almost no time-dependency of PqsD inhibition
(2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-[[4-(2-nitrophenyl)-4-oxobutyl]amino]-3-oxopropyl)butanamide
-
0.05 mM, 18% inhibition
(2R)-2,4-dihydroxy-N-(3-[[4-hydroxy-4-(2-nitrophenyl)butyl]amino]-3-oxopropyl)-3,3-dimethylbutanamide
-
0.05 mM, 95% inhibition
(S)-(2-nitrophenyl)(phenyl)methanol
most active compound of the series, capable of reducing the HHQ and PQS levels as well as the biofilm volume in Pseudomonas aeruginosa PA14 without affecting cell viability. The (S)-enantiomer has a pronounced entropic binding profile. Docking results show a short hydrogen bond between NO2 and NH of Ser317. The hydroxyl group is involved in different interactions, either facing toward Asn287 or His256/Cys112
1-(2-nitrophenyl)propan-1-ol
best inhibitor in the cellular test
2-[[3-(diethylsulfamoyl)-4-ethylbenzoyl]amino]benzoic acid
-
0.05 mM, 39% inhibition
2-[[3-(diethylsulfamoyl)benzoyl]amino]-5-(trifluoromethyl)benzoic acid
-
-
2-[[3-(diethylsulfamoyl)benzoyl]amino]-6-methoxybenzoic acid
-
0.05 mM, 44% inhibition
2-[[3-(dimethylsulfamoyl)benzoyl]amino]benzoic acid
-
0.05 mM, 35% inhibition
2-[[3-(morpholin-4-ylsulfonyl)benzoyl]amino]benzoic acid
-
0.05 mM, 16% inhibition
2-[[3-(pyrrolidin-1-ylsulfonyl)benzoyl]amino]benzoic acid
-
0.05 mM, 47% inhibition
2-[[4-bromo-3-(diethylsulfamoyl)benzoyl]amino]-5-fluorobenzoic acid
-
-
3'-carbamoyl-4-[[3-(diethylsulfamoyl)benzoyl]amino]biphenyl-3-carboxylic acid
-
-
3-(3,4-dihydroxyphenyl)-N-methylpropanamide
potent inhibitor, completely inactive in the cell-based assay
4'-carbamoyl-4-[[3-(diethylsulfamoyl)benzoyl]amino]biphenyl-3-carboxylic acid
-
-
4-[[3-(diethylsulfamoyl)benzoyl]amino]biphenyl-3,3'-dicarboxylic acid
-
-
4-[[3-(diethylsulfamoyl)benzoyl]amino]biphenyl-3,4'-dicarboxylic acid
-
-
5-bromo-2-[[4-bromo-3-(diethylsulfamoyl)benzoyl]amino]benzoic acid
-
-
N-(2-chloro-6-methylphenyl)biphenyl-4-carboxamide
strong inhibition of enzyme, without inhibition of RNA polymerase
N-[2-[hydroxy(2-nitrophenyl)methyl]phenyl]acetamide
-
0.05 mM, 93% inhibition
N-[3-[hydroxy(2-nitrophenyl)methyl]phenyl]acetamide
-
0.05 mM, 99% inhibition
N-[4-hydroxy-4-(2-nitrophenyl)butyl]acetamide
-
0.05 mM, 99% inhibition
N-[4-[hydroxy(2-nitrophenyl)methyl]phenyl]acetamide
-
0.05 mM, 98% inhibition
additional information
-
identification of a class of PqsD inhibitors using a ligand-based approach. Simplification and rigidization leads to fragments with high ligand efficiencies. These small molecules repress HHQ and PQS production and biofilm formation in Pseudomonas aeruginosa. This validates PqsD as a target for the development of anti-infectives. No inhibition by 0.05 mM (3-[[4-(2-aminophenyl)-4-oxobutyl]amino]-3-oxopropyl)-2,4-dihydroxy-3,3-dimethylbutanamide, (2R)-N-(3-[[4-(2-aminophenyl)-4-hydroxybutyl]amino]-3-oxopropyl)-2,4-dihydroxy-3,3-dimethylbutanamide, (2-nitrophenyl)(phenyl)methanone, 1-(2-nitrophenyl)-1-phenylethanol and 2,2,2-trifluoro-1-(2-nitrophenyl)-1-phenylethanol
-
additional information
-
optimization and characterization of 2-benzamidobenzoic acids as PqsD inhibitors. Structural modifications show that both the carboxylic acid ortho to the amide and 3'-sulfonamide are essential for binding. Introduction of substituents in the anthranilic part of the molecule results in compounds with IC50 values in the low micromolar range. This class of inhibitors does not bind into the active center of PqsD but in the ACoA channel, preventing the substrate from accessing the active site
-
additional information
evaluation of selected substrates of the Medicago sativa chalcone synthase CHS2 as potential inhibitors of PqsD. Catechol derivatives possessing an ester moiety are able to reduce the production of 2-heptyl-4(1H)-quinolone in the bacterial cultures without affecting cellular growth
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.599
2-aminobenzoyl-CoA
-
pH and temperature not specified in the publication
0.0487
malonyl-CoA
-
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
2-aminobenzoyl-CoA
-
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
(2-nitrophenyl)(phenyl)methanol
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0059
(2-nitrophenyl)(thiophen-3-yl)methanol
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
7.9
(2R)-2,4-dihydroxy-N-(3-[[4-hydroxy-4-(2-nitrophenyl)butyl]amino]-3-oxopropyl)-3,3-dimethylbutanamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0032
(S)-(2-nitrophenyl)(phenyl)methanol
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
0.0011
1-(2-nitrophenyl)propan-1-ol
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
4.3
1-[methoxy(phenyl)methyl]-2-nitrobenzene
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.065
2-(4-bromo-3-diethylsulfamoylbenzoylamino)benzoate
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0165
2-([3-[benzyl(ethyl)sulfamoyl]benzoyl]amino)benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.039
2-chloro-6-[[3-(diethylsulfamoyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
14.8
2-nitrophenyl phenyl sulfone
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.035
2-[(2-phenoxybiphenyl-4-carbonyl)amino]benzoate
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.044
2-[(3-sulfamoylbenzoyl)amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0148
2-[[3-(azepan-1-ylsulfonyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0273
2-[[3-(diethylsulfamoyl)-4-methylbenzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.008
2-[[3-(diethylsulfamoyl)benzoyl]amino]-4-fluorobenzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0063
2-[[3-(diethylsulfamoyl)benzoyl]amino]-4-nitrobenzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0124
2-[[3-(diethylsulfamoyl)benzoyl]amino]-5-(trifluoromethyl)benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0114
2-[[3-(diethylsulfamoyl)benzoyl]amino]-5-fluorobenzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0184
2-[[3-(diethylsulfamoyl)benzoyl]amino]-5-methylbenzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0089
2-[[3-(diethylsulfamoyl)benzoyl]amino]-5-nitrobenzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.025
2-[[3-(diethylsulfamoyl)benzoyl]amino]-6-fluorobenzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0012
2-[[3-(diethylsulfamoyl)benzoyl]amino]-6-hydroxybenzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0198
2-[[3-(diethylsulfamoyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0054
2-[[3-(dipropylsulfamoyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0144
2-[[3-(piperidin-1-ylsulfonyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0066
2-[[4-bromo-3-(diethylsulfamoyl)benzoyl]amino]-5-fluorobenzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0069
2-[[4-bromo-3-(diethylsulfamoyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0038
3'-carbamoyl-4-[[3-(diethylsulfamoyl)benzoyl]amino]biphenyl-3-carboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.023
3-(3,4-dihydroxyphenyl)-N-methylpropanamide
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
0.0019
4'-carbamoyl-4-[[3-(diethylsulfamoyl)benzoyl]amino]biphenyl-3-carboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0094
4-chloro-2-[[3-(diethylsulfamoyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0015
4-[[3-(diethylsulfamoyl)benzoyl]amino]biphenyl-3,3'-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0027
4-[[3-(diethylsulfamoyl)benzoyl]amino]biphenyl-3,4'-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.003
4-[[3-(diethylsulfamoyl)benzoyl]amino]biphenyl-3-carboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0255
5-bromo-2-[[3-(diethylcarbamoyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.009
5-bromo-2-[[3-(diethylsulfamoyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.013
5-bromo-2-[[4-(diethylsulfamoyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0038
5-bromo-2-[[4-bromo-3-(diethylsulfamoyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.026
5-cyano-2-[[3-(diethylsulfamoyl)benzoyl]amino]benzoic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0059
benzyl 3-(3,4-dihydroxyphenyl)propanoate
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
0.02
methyl 3-(3,4-dihydroxyphenyl)propanoate
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
0.0062
N-(2-chloro-6-methylphenyl)biphenyl-4-carboxamide
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
6.2
N-[2-[hydroxy(2-nitrophenyl)methyl]phenyl]acetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
9
N-[3-[hydroxy(2-nitrophenyl)methyl]phenyl]acetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
7.8
N-[4-(2-nitrophenyl)-4-oxobutyl]acetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
4.3
N-[4-hydroxy-4-(2-nitrophenyl)butyl]acetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
6.4
N-[4-[hydroxy(2-nitrophenyl)methyl]phenyl]acetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q9I4X2: 2-heptyl-4(1H)-quinolone synthase subunit PqsB, Q9I4X1: 2-heptyl-4(1H)-quinolone synthase subunit PqsC
Q9I4X2; Q9I4X1
SwissProt
brenda
Q9I4X2: 2-heptyl-4(1H)-quinolone synthase subunit PqsB, Q9I4X1: 2-heptyl-4(1H)-quinolone synthase subunit PqsC
Q9I4X2; Q9I4X1
SwissProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
Q9I4X2; Q9I4X1
PqsBC, a key enzyme in the biosynthesis of the quorum-sensing signal molecules 2-heptyl-4(1H)-quinolone and Pseudomonas quinolone signal
metabolism
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PqsBC, a key enzyme in the biosynthesis of the quorum-sensing signal molecules 2-heptyl-4(1H)-quinolone and Pseudomonas quinolone signal
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physiological function
PqsD is a quinolone signal biosynthetic enzyme
physiological function
-
synthesis of 2,4-dihydroxyquinoline, an extracellular metabolite produced by Pseudomonas aeruginosa and secreted into growth medium in stationary phase. The enzyme is essential for Pseudomonas quinolone signal synthesis
physiological function
4-hydroxy-2-alkylquinoline biosynthesis, which requires the PqsABCD enzymes, proceeds by a two-step pathway: PqsD mediates the synthesis of 2-aminobenzoylacetate from anthraniloyl-coenzyme A and malonyl-coenzyme A, then the decarboxylating coupling of 2-aminobenzoylacetate to an octanoate group linked to PqsC produces 4-hydroxy-2-heptylquinoline, the direct precursor of 3,4-dihydroxy-2-heptylquinoline. PqsB is tightly associated with PqsC and required for the second step. None of the pqsA-, pqsB-, pqsC-, and pqs- mutants produces measurable amounts of 4-hydroxy-2-alkylquinolines
physiological function
-
4-hydroxy-2-alkylquinoline biosynthesis, which requires the PqsABCD enzymes, proceeds by a two-step pathway: PqsD mediates the synthesis of 2-aminobenzoylacetate from anthraniloyl-coenzyme A and malonyl-coenzyme A, then the decarboxylating coupling of 2-aminobenzoylacetate to an octanoate group linked to PqsC produces 4-hydroxy-2-heptylquinoline, the direct precursor of 3,4-dihydroxy-2-heptylquinoline. PqsB is tightly associated with PqsC and required for the second step. None of the pqsA-, pqsB-, pqsC-, and pqs- mutants produces measurable amounts of 4-hydroxy-2-alkylquinolines
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PQSC_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
348
0
38239
Swiss-Prot
-
A0A0H2Z7U1_PSEAB
Pseudomonas aeruginosa (strain UCBPP-PA14)
337
0
36407
TrEMBL
-
PQSD_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
337
0
36379
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulations suggest a nucleophilic attack of the deprotonated sulfur of Cys112 at the carbonyl carbon of ACoA and a switch in the protonation pattern of His257 whereby Ndelta is protonated and the proton of Nepsilon is shifted to the sulfur of CoA during the reaction. In the N287A mutant anthraniloyl remains covalently bound to C112, further supporting that N87 does not take part in the cleavage of anthraniloyl-CoA
sitting drop vapor diffusion method, PqsBC(C129A) crystallized in space group P2(1)2(1)2(1) and the structure is determined to 2 A resolution, revealing that PqsB and PqsC have a pseudo-2-fold symmetry
Q9I4X2; Q9I4X1
sitting drop vapor diffusion method. Several crystal structures of the enzyme including that of the PqsD-anthranilate covalent intermediate and the inactive Cys112Ala active site mutant in complex with anthranilate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C112A
C112S
H257F
N287A
inactive, anthraniloyl remains covalently bound to C112, further supporting that N87 does not take part in the cleavage of anthraniloyl-CoA
S317F
C112A
-
binding behavior towards inhibitors is different from wild-type enzyme
C112A
the C112A mutant is inactive although it still reversibly binds anthraniloyl-CoA
H257F
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binding behavior towards inhibitors is different from wild-type enzyme
S317F
-
binding behavior towards inhibitors is different from wild-type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
4-hydroxy-2(1H)-quinolone is produced by Escherichia coli coexpressing PqsA and PqsD
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the pqsB and pqsC genes of are cloned into plasmid pET28b and expresssed in Escherichia coli Rosetta2(DE3)
Q9I4X2; Q9I4X1
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bera, A.K.; Atanasova, V.; Robinson, H.; Eisenstein, E.; Coleman, J.P.; Pesci, E.C.; Parsons, J.F.
Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate
Biochemistry
48
8644-8655
2009
Pseudomonas aeruginosa (P20582)
brenda
Steinbach, A.; Maurer, C.K.; Weidel, E.; Henn, C.; Brengel, C.; Hartmann, R.W.; Negri, M.
Molecular basis of HHQ biosynthesis: molecular dynamics simulations, enzyme kinetic and surface plasmon resonance studies
BMC Biophys.
6
10
2013
Pseudomonas aeruginosa
brenda
Pistorius, D.; Ullrich, A.; Lucas, S.; Hartmann, R.W.; Kazmaier, U.; Müller, R.
Biosynthesis of 2-Alkyl-4(1H)-quinolones in Pseudomonas aeruginosa: potential for therapeutic interference with pathogenicity
Chembiochem
12
850-853
2011
Pseudomonas aeruginosa
brenda
Storz, M.P.; Maurer, C.K.; Zimmer, C.; Wagner, N.; Brengel, C.; de Jong, J.C.; Lucas, S.; Müsken, M.; Häussler, S.; Steinbach, A.; Hartmann, R.W.
Validation of PqsD as an anti-biofilm target in Pseudomonas aeruginosa by development of small-molecule inhibitors
J. Am. Chem. Soc.
134
16143-16146
2012
Pseudomonas aeruginosa
brenda
Zhang, Y.M.; Frank, M.W.; Zhu, K.; Mayasundari, A.; Rock, C.O.
PqsD is responsible for the synthesis of 2,4-dihydroxyquinoline, an extracellular metabolite produced by Pseudomonas aeruginosa
J. Biol. Chem.
283
28788-28794
2008
Pseudomonas aeruginosa
brenda
Weidel, E.; de Jong, J.C.; Brengel, C.; Storz, M.P., Braunshausen, A.; Negri, M.; Plaza, A.; Steinbach, A.; Müller, R.; Hartmann, R.W.
Structure optimization of 2-benzamidobenzoic acids as PqsD inhibitors for Pseudomonas aeruginosa infections and elucidation of binding mode by SPR, STD NMR, and molecular docking
J. Med. Chem.
56
6146-6155
2013
Pseudomonas aeruginosa
brenda
Storz, M.P.; Brengel, C.; Weidel, E.; Hoffmann, M.; Hollemeyer, K.; Steinbach, A.; Mueller, R.; Empting, M.; Hartmann, R.W.
Biochemical and biophysical analysis of a chiral PqsD inhibitor revealing tight-binding behavior and enantiomers with contrary thermodynamic signatures
ACS Chem. Biol.
8
2794-2801
2013
Pseudomonas aeruginosa (A0A0H2Z7U1)
brenda
Dulcey, C.E.; Dekimpe, V.; Fauvelle, D.A.; Milot, S.; Groleau, M.C.; Doucet, N.; Rahme, L.G.; Lepine, F.; Deziel, E.
The end of an old hypothesis: the Pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids
Chem. Biol.
20
1481-1491
2013
Pseudomonas aeruginosa (A0A0H2Z7U1), Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2Z7U1)
brenda
Hinsberger, S.; de Jong, J.C.; Groh, M.; Haupenthal, J.; Hartmann, R.W.
Benzamidobenzoic acids as potent PqsD inhibitors for the treatment of Pseudomonas aeruginosa infections
Eur. J. Med. Chem.
76
343-351
2014
Pseudomonas aeruginosa (P20582)
brenda
Allegretta, G.; Weidel, E.; Empting, M.; Hartmann, R.W.
Catechol-based substrates of chalcone synthase as a scaffold for novel inhibitors of PqsD
Eur. J. Med. Chem.
90
351-359
2015
Pseudomonas aeruginosa (P20582)
brenda
Hutter, M.C.; Brengel, C.; Negri, M.; Henn, C.; Zimmer, C.; Hartmann, R.W.; Empting, M.; Steinbach, A.
Mechanistic details for anthraniloyl transfer in PqsD: the initial step in HHQ biosynthesis
J. Mol. Model.
20
2255
2014
Pseudomonas aeruginosa (P20582)
brenda
Storz, M.P.; Allegretta, G.; Kirsch, B.; Empting, M.; Hartmann, R.W.
From in vitro to in cellulo: structure-activity relationship of (2-nitrophenyl)methanol derivatives as inhibitors of PqsD in Pseudomonas aeruginosa
Org. Biomol. Chem.
12
6094-6104
2014
Pseudomonas aeruginosa (P20582)
brenda
Drees, S.; Li, C.; Prasetya, F.; Saleem, M.; Dreveny, I.; Williams, P.; Hennecke, U.; Emsley, J.; Fetzner, S.
PqsBC, a condensing enzyme in the biosynthesis of the pseudomonas aeruginosa quinolone signal Crystal structure, inhibition, and reaction mechanism
J. Biol. Chem.
291
6610-6624
2016
Pseudomonas aeruginosa (Q9I4X2 AND Q9I4X1), Pseudomonas aeruginosa ATCC 15692 (Q9I4X2 AND Q9I4X1)
brenda
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