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Enzyme Nomenclature
Information on EC 2.3.1.262 - anthraniloyl-CoA anthraniloyltransferase
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EC Tree
2.3.1.262 anthraniloyl-CoA anthraniloyltransferaseIUBMB Comments
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the synthesis of the secondary metabolites 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone. The enzyme transfers an anthraniloyl group from anthraniloyl-CoA to an internal L-cysteine residue, followed by its transfer to malonyl-CoA to produce a short-lived product that can cyclize spontaneously to form 4-hydroxy-2(1H)-quinolone. However, when EC 3.1.2.32, 2-aminobenzoylacetyl-CoA thioesterase, is present, it removes the CoA moiety from the product, forming the stable (2-aminobenzoyl)acetate.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-heptyl-4(1H)-quinolone synthase
PqsD
PqsD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anthraniloyl-CoA + L-cysteinyl-[PqsD protein] = S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA
(1a)
-
-
-
anthraniloyl-CoA + malonyl-CoA = 2-aminobenzoylacetyl-CoA + CoA + CO2
overall reaction
-
-
-
S-anthraniloyl-L-cysteinyl-[PqsD protein] + malonyl-CoA = 2-aminobenzoylacetyl-CoA + CO2 + L-cysteinyl-[PqsD protein]
(1b)
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
anthraniloyl-CoA:malonyl-CoA anthraniloyltransferase
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the synthesis of the secondary metabolites 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone. The enzyme transfers an anthraniloyl group from anthraniloyl-CoA to an internal L-cysteine residue, followed by its transfer to malonyl-CoA to produce a short-lived product that can cyclize spontaneously to form 4-hydroxy-2(1H)-quinolone. However, when EC 3.1.2.32, 2-aminobenzoylacetyl-CoA thioesterase, is present, it removes the CoA moiety from the product, forming the stable (2-aminobenzoyl)acetate.
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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
anthraniloyl-CoA + L-cysteinyl-[PqsD protein]
S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA
-
-
-
?
anthraniloyl-CoA + malonyl-CoA
2,4-dihydroxyquinoline + 2 CoA + CO2 + ?
-
in vitro overall reaction
-
?
S-anthraniloyl-L-cysteinyl-[PqsD protein] + malonyl-CoA
2-aminobenzoylacetyl-CoA + CO2 + L-cysteinyl-[PqsD protein]
-
-
-
?
additional information
?
-
initial catalytic step of PqsD is the transfer of the anthraniloyl moiety to residue Cys112 under hydrolysis of the anthraniloyl-CoA thioester. The second step in the reaction that leads to Cys112-anthraniloyl and CoA is a concerted reaction mechanism. The deprotonated sulfur atom of Cys112 performs a nucleophilic attack at the carbonyl carbon of anthraniloyl-CoA while the proton at Nepsilon of His257 is simultaneously shifted to the sulfur atom of CoA. During the reaction, His257 switches its protonation pattern. Only Nepsilon is protonated in the reactant state, whereas the uptake of a proton at Ndelta to deprotonation of Cys112 leads to a doubly protonated (positively charged) intermediate. From there, the proton at Nepsilon is subsequently transferred to the sulfur of CoA, leading to a net neutral product
-
-
?
anthraniloyl-CoA + malonyl-CoA
2-aminobenzoylacetyl-CoA + CoA + CO2
-
-
-
?
anthraniloyl-CoA + malonyl-CoA
2-aminobenzoylacetyl-CoA + CoA + CO2
-
overall reaction
-
?
anthraniloyl-CoA + malonyl-CoA
2-aminobenzoylacetyl-CoA + CoA + CO2
-
-
-
?
anthraniloyl-CoA + malonyl-CoA
2-aminobenzoylacetyl-CoA + CoA + CO2
-
-
-
?
anthraniloyl-CoA + malonyl-CoA
2-aminobenzoylacetyl-CoA + CoA + CO2
-
-
-
?
anthraniloyl-CoA + malonyl-CoA
2-aminobenzoylacetyl-CoA + CoA + CO2
-
-
-
?
anthraniloyl-CoA + malonyl-CoA
2-aminobenzoylacetyl-CoA + CoA + CO2
-
-
-
?
anthraniloyl-CoA + malonyl-CoA
2-aminobenzoylacetyl-CoA + CoA + CO2
-
-
-
?
anthraniloyl-CoA + malonyl-CoA
2-aminobenzoylacetyl-CoA + CoA + CO2
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-2,4-dihydroxy-N-(3-[[4-hydroxy-4-(2-nitrophenyl)butyl]amino]-3-oxopropyl)-3,3-dimethylbutanamide
-
(E)-1-(2-chloro-8-methylquinolin-3-yl)-N-[3-fluoro-4-(morpholin-4-yl)phenyl]methanimine
-
(E)-1-(2-chloroquinolin-3-yl)-N-[3-fluoro-4-(morpholin-4-yl)phenyl]methanimine
-
1-(1-aminonaphthalen-2-yl)-2-chloroethan-1-one
strong inhibition
1-(7-amino-2,3-dihydro-1,4-benzodioxin-6-yl)-2-chloroethan-1-one
strong inhibition
2-(3,4-dichlorobenzene-1-sulfonyl)-4-(1H-tetrazol-1-yl)pyrimidine
-
2-(methanesulfonyl)-4-(4-phenyl-1H-1,2,3-triazol-1-yl)pyrimidine
-
2-(methanesulfonyl)-4-phenoxy-6-(1H-1,2,3-triazol-1-yl)pyrimidine
-
2-chloro-N-(3-chloro-2-methylphenyl)acetamide
strong inhibition
2-[(biphenyl-4-ylcarbonyl)amino]-3-chlorobenzoic acid
-
strong inhibition, without inhibiting RNA polymerase
2-[3-hydroxy-3-(2-nitrophenyl)propyl]-1H-isoindole-1,3(2H)-dione
-
3,5-dichloro-N-(1-chloro-3-methyl-2-oxopentan-3-yl)-4-methylbenzamide
-
3-(3-carboxypropanamido)-5-(4-methoxyphenyl)thiophene-2-carboxylic acid
-
3-([[(1S)-1-carboxy-2-phenylethyl]carbamoyl]amino)-7-methoxy-4,5-dihydronaphtho[1,2-b]thiophene-2-carboxylic acid
-
3-([[(1S)-1-carboxy-3-phenylpropyl]carbamoyl]amino)-5-(4-methoxyphenyl)thiophene-2-carboxylic acid
-
3-([[(S)-carboxy(phenyl)methyl]carbamoyl]amino)-5-(4-methoxyphenyl)thiophene-2-carboxylic acid
-
3-[[benzyl(ethyl)carbamoyl]amino]-5-(4-methoxyphenyl)thiophene-2-carboxylic acid
-
4-[3-(diethylsulfamoyl)benzamido][1,1'-biphenyl]-3-carboxylic acid
-
N-([(5R)-3-[3-fluoro-4-(morpholin-4-yl)phenyl]-2-oxo-1,3-oxazolidin-5-yl]methyl)acetamide
-
N-([2-carboxy-5-[4'-(hydroxymethyl)[1,1'-biphenyl]-4-yl]thiophen-3-yl]carbamoyl)-L-phenylalanine
-
N-([2-carboxy-5-[4-(2-chloroacetamido)phenyl]thiophen-3-yl]carbamoyl)-L-phenylalanine
-
N-[(2-carboxy-5-phenylthiophen-3-yl)carbamoyl]-L-phenylalanine
-
N-[(2-carboxy-5-[4'-[hydroxy(2-nitrophenyl)methyl][1,1'-biphenyl]-4-yl]thiophen-3-yl)carbamoyl]-L-phenylalanine
-
N-[[2-carboxy-5-(4-hydroxyphenyl)thiophen-3-yl]carbamoyl]-L-phenylalanine
-
N-[[2-carboxy-5-(4-methoxy-2-methylphenyl)thiophen-3-yl]carbamoyl]-L-phenylalanine
-
N-[[2-carboxy-5-(4-methoxyphenyl)thiophen-3-yl]carbamoyl]-4-chloro-L-phenylalanine
-
N-[[2-carboxy-5-(4-methoxyphenyl)thiophen-3-yl]carbamoyl]-L-phenylalanine
-
N-[[2-carboxy-5-(4-methoxyphenyl)thiophen-3-yl]carbamoyl]-L-tyrosine
-
N-[[3-(furan-2-yl)-1H-pyrazol-5-yl]methyl]-2-(4-methylpiperazin-1-yl)pyrimidin-4-amine
-
additional information
inhibitor development targeting enzyme PqsD, development of a competitive in situ labeling strategy using an electrophilic activity-based probe and target protein expressing Escherichia coli cells
-
(2-nitrophenyl)(phenyl)methanol
-
at a concentration of 250 microM, both the 2-heptyl-4-hydroxyquinoline and Pseudomonas quinolone signal levels are strongly reduced by 77 and 42%, respectively, in Pseudomonas aeruginosa PA14 cultures. The 2,4-dihydroxyquinoline level increases in the presence of the compound. Addition of the compound to a 24 h old biofilm reduces the biovolume of the biofilm by 38% within a 24 h incubation period
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0079
(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
0.0156
(E)-1-(2-chloro-8-methylquinolin-3-yl)-N-[3-fluoro-4-(morpholin-4-yl)phenyl]methanimine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0129
(E)-1-(2-chloroquinolin-3-yl)-N-[3-fluoro-4-(morpholin-4-yl)phenyl]methanimine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0012
1-(1-aminonaphthalen-2-yl)-2-chloroethan-1-one
Pseudomonas aeruginosa
pH not specified in the publication, 37°C
0.0019
1-(2-aminophenyl)-2-chloroethan-1-one
Pseudomonas aeruginosa
pH not specified in the publication, 37°C
0.0011
1-(2-nitrophenyl)propan-1-ol
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0022
1-(7-amino-2,3-dihydro-1,4-benzodioxin-6-yl)-2-chloroethan-1-one
Pseudomonas aeruginosa
pH not specified in the publication, 37°C
0.0004
2-(3,4-dichlorobenzene-1-sulfonyl)-4-(1H-tetrazol-1-yl)pyrimidine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0017
2-(benzenesulfonyl)-4-(1H-tetrazol-1-yl)pyrimidine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0017
2-(hexane-1-sulfonyl)-4-(1H-1,2,3-triazol-1-yl)pyrimidine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0032
2-(methanesulfonyl)-4-phenoxy-6-(1H-1,2,3-triazol-1-yl)pyrimidine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0025
2-chloro-1-(1H-indol-7-yl)ethan-1-one
Pseudomonas aeruginosa
pH not specified in the publication, 37°C
0.0013
2-chloro-1-(2,4-difluorophenyl)ethan-1-one
Pseudomonas aeruginosa
pH not specified in the publication, 37°C
0.0018
2-chloro-1-phenylethan-1-one
Pseudomonas aeruginosa
pH not specified in the publication, 37°C
0.0021
2-chloro-N-(3-chloro-2-methylphenyl)acetamide
Pseudomonas aeruginosa
pH not specified in the publication, 37°C
0.155
2-chloro-N-(4-methylphenyl)acetamide
Pseudomonas aeruginosa
pH not specified in the publication, 37°C
0.0062
2-[(biphenyl-4-ylcarbonyl)amino]-3-chlorobenzoic acid
Pseudomonas aeruginosa
-
pH not specified in the publication, temperature not specified in the publication
0.0062
2-[([1,1'-biphenyl]-4-carbonyl)amino]-3-chlorobenzoic acid
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0013
2-[([1,1'-biphenyl]-4-carbonyl)amino]benzoic acid
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0012
2-[3-(diethylsulfamoyl)benzamido]-6-hydroxybenzoic acid
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0003
2-[3-hydroxy-3-(2-nitrophenyl)propyl]-1H-isoindole-1,3(2H)-dione
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.027
3-(3,4-dihydroxyphenyl)propanoic acid
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.007
3-(3-carboxypropanamido)-5-(4-methoxyphenyl)thiophene-2-carboxylic acid
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0237
3-([[(1S)-1-carboxy-2-phenylethyl]carbamoyl]amino)-7-methoxy-4,5-dihydronaphtho[1,2-b]thiophene-2-carboxylic acid
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.006
3-[[benzyl(ethyl)carbamoyl]amino]-5-(4-methoxyphenyl)thiophene-2-carboxylic acid
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0003
4-[3-(diethylsulfamoyl)benzamido][1,1'-biphenyl]-3-carboxylic acid
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0059
benzyl 3-(3,4-dihydroxyphenyl)propanoate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.051
methyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0079
methyl 4-(3,4-dihydroxyphenyl)butanoate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0159
N-([(5R)-3-[3-fluoro-4-(morpholin-4-yl)phenyl]-2-oxo-1,3-oxazolidin-5-yl]methyl)acetamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.00036
N-([2-carboxy-5-[4'-(hydroxymethyl)[1,1'-biphenyl]-4-yl]thiophen-3-yl]carbamoyl)-L-phenylalanine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.002
N-([2-carboxy-5-[4-(2-chloroacetamido)phenyl]thiophen-3-yl]carbamoyl)-L-phenylalanine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0038
N-[(2-carboxy-5-phenylthiophen-3-yl)carbamoyl]-L-phenylalanine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0014
N-[(2-carboxy-5-[4'-[hydroxy(2-nitrophenyl)methyl][1,1'-biphenyl]-4-yl]thiophen-3-yl)carbamoyl]-L-phenylalanine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0043
N-[4-hydroxy-4-(2-nitrophenyl)butyl]acetamide
Pseudomonas aeruginosa
-
pH not specified in the publication, temperature not specified in the publication
0.0216
N-[[2-carboxy-5-(4-hydroxyphenyl)thiophen-3-yl]carbamoyl]-L-phenylalanine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0075
N-[[2-carboxy-5-(4-methoxy-2-methylphenyl)thiophen-3-yl]carbamoyl]-L-phenylalanine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0138
N-[[2-carboxy-5-(4-methoxyphenyl)thiophen-3-yl]carbamoyl]-4-chloro-L-phenylalanine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0005
N-[[2-carboxy-5-(4-methoxyphenyl)thiophen-3-yl]carbamoyl]-L-phenylalanine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.029
N-[[2-carboxy-5-(4-methoxyphenyl)thiophen-3-yl]carbamoyl]-L-tyrosine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0086
propan-2-yl 3-(3,4-dihydroxyphenyl)propanoate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0032
(2-nitrophenyl)(phenyl)methanol
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0032
(2-nitrophenyl)(phenyl)methanol
Pseudomonas aeruginosa
-
pH not specified in the publication, temperature not specified in the publication
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
PqsD is an enzyme essential for the Pseudomonas aeruginosa quorum-sensing apparatus, which catalyzes the final and key step in the biosynthesis of 4-hydroxy-2-heptylquinolone, which is a signal molecule of the Pseudomonas aeruginosa quorum-sensing system
physiological function
physiological function
4-hydroxy-2-alkylquinolines biosynthesis requires the PqsABCD enzymes and proceeds by a two-step pathway: First, PqsD mediates the synthesis of 2-aminobenzoylacetate from anthraniloyl-CoA and malonyl-CoA, then the decarboxylating coupling of 2-aminobenzoylacetate to an octanoate group linked to PqsC produces 4-hydroxy-2-heptylquinoline, the direct precursor of Pseudomonas quinolone signal. PqsB is tightly associated with PqsC and required for the second step
physiological function
in addition to PqsABCD, PqsE has a role in 2-heptyl-4(1H)-quinolone synthesis. PqsE acts as thioesterase, hydrolyzing the biosynthetic intermediate 2-aminobenzoylacetyl-coenzyme A formed by PsqD to form 2-aminobenzoylacetate, the precursor of 2-heptyl-4(1H)-quinolone and 2-aminoacetophenone
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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). PQSD_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
337
0
36379
Swiss-Prot
-
A0A5K1JT49_9APHY
229
0
24504
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the enzyme including the PqsD-anthranilate covalent intermediate and the inactive Cys112Ala active site mutant in complex with anthranilate. The crystallographic asymmetric unit contains a PqsD dimer. The PqsD monomer is composed of two nearly identical about 170 residue alphabetalaphabeta domains. Anthranilate-liganded residue Cys112 is positioned deep in the protein interior at the bottom of a 15 A long channel while a second anthraniloyl-CoA molecule is waiting in the cleft leading to the protein surface. Cys112, His257, and Asn287 form the FabH-like catalytic triad of PqsD
molecular dynamics simulations reveal a nucleophilic attack of the deprotonated sulfur of residue Cys112 at the carbonyl carbon of anthraniloyl-coenzyme A 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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C112A
additional information
C112A
mutant is inactive although it still reversibly binds anthraniloyl-CoA
additional information
development of a competitive in situ labeling strategy using an electrophilic activity-based probe and target protein expressing Escherichia coli cells
additional information
-
development of a competitive in situ labeling strategy using an electrophilic activity-based probe and target protein expressing Escherichia coli cells
-
additional information
-
development of a competitive in situ labeling strategy using an electrophilic activity-based probe and target protein expressing Escherichia coli cells
-
additional information
-
development of a competitive in situ labeling strategy using an electrophilic activity-based probe and target protein expressing Escherichia coli cells
-
additional information
-
development of a competitive in situ labeling strategy using an electrophilic activity-based probe and target protein expressing Escherichia coli cells
-
additional information
-
development of a competitive in situ labeling strategy using an electrophilic activity-based probe and target protein expressing Escherichia coli cells
-
additional information
-
development of a competitive in situ labeling strategy using an electrophilic activity-based probe and target protein expressing Escherichia coli cells
-
additional information
-
development of a competitive in situ labeling strategy using an electrophilic activity-based probe and target protein expressing Escherichia coli cells
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
antivirulence concepts through the inhibition of PqsD in the treatment of bacterial infections
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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
Storz, M.P.; Maurer, C.K.; Zimmer, C.; Wagner, N.; Brengel, C.; de Jong, J.C.; Lucas, S.; Msken, M.; Hussler, 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
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 (P20582)
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
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
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 (P20582)
brenda
Zhou, Z.; Ma, S.
Recent advances in the discovery of PqsD inhibitors as antimicrobial agents
ChemMedChem
12
420-425
2017
Pseudomonas aeruginosa (P20582)
brenda
Prothiwa, M.; Englmaier, F.; Boettcher, T.
Competitive live-cell profiling strategy for discovering inhibitors of the quinolone biosynthesis of Pseudomonas aeruginosa
J. Am. Chem. Soc.
140
14019-14023
2018
Pseudomonas aeruginosa (P20582), Pseudomonas aeruginosa ATCC 15692 (P20582), Pseudomonas aeruginosa 1C (P20582), Pseudomonas aeruginosa PRS 101 (P20582), Pseudomonas aeruginosa DSM 22644 (P20582), Pseudomonas aeruginosa CIP 104116 (P20582), Pseudomonas aeruginosa LMG 12228 (P20582), Pseudomonas aeruginosa JCM 14847 (P20582)
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Release 2023.1 (January 2023)
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