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Information on EC 6.2.1.32 - anthranilate-CoA ligase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9I4X3
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6.2.1.32 anthranilate-CoA ligaseSpecify your search results
Word Map
- 6.2.1.32
- 2-aminobenzoyl-coa
-
denitrifying
-
alicyclic
- ligases
- aeruginosa
- thioesters
- acyl-coa
- flavoproteins
-
nosocomial
- salicylate
- nitrate
- pyrophosphate
-
flavoenzyme
- monooxygenase
- drug development
- synthesis
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2-aminobenzoate-coa ligase, anthranilate-coa ligase, 2-aminobenzoate-coenzyme a ligase, 2-aminobenzoate coenzyme a ligase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-aminobenzoate coenzyme A ligase
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2-aminobenzoate-CoA ligase
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2-aminobenzoate-coenzyme A ligase
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synthetase, anthraniloyl coenzyme A
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + anthranilate + CoA = AMP + diphosphate + anthraniloyl-CoA
reaction via anthraniloyl-AMP intermediate. The catalytic cycle of PqsA consists of two steps: in the first half-reaction of PqsA (adenylation), anthranilate is activated with ATP/Mg2+ to produce the intermediate anthraniloyl-AMP with the release of diphosphate. The aryl moiety is then transferred to the acceptor molecule CoA to form anthraniloyl-CoA in the second half-reaction (thioester formation). The two half-reactions are cooperatively catalyzed by a large N-terminal domain and a smaller C-terminal domain separated by a flexible linker, the latter undergoes large conformational rearrangements in the course of the catalytic cycle
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
forming of carbon sulfur bonds
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
anthranilate:CoA ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY
112692-58-7
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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
ATP + anthranilate + CoA
AMP + diphosphate + anthraniloyl-CoA
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?
ATP + anthranilate + CoA
AMP + diphosphate + anthranilyl-CoA
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ATP + anthranilate + CoA
AMP + diphosphate + anthranilyl-CoA
the Pseudomonas quinolone signal PQS is a 3-hydroxy-4-quinolone with a 2-alkyl substitution, which is synthesized by the condensation of anthranilic acid with a 3-keto-fatty acid, pathway for PQS biosynthesis, anthranilate is activated by PqsA to form anthraniloyl-CoA, and this is condensed with 2-oxo-decanoyl-ACP which is recruited from the fatty acid biosynthetic pathway, overview
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additional information
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6-fluoroanthraniloyl-AMP (6FABA-AMP), an inhibitor of PQS biosynthesis, is a good substrate of enzyme PqsA, enzyme binding structure analysis of 6-fluoroanthraniloyl-AMP and anthraniloyl-AMP, overview. 6FABA-AMP binds to PqsANTD in a similar way to anthraniloyl-AMP, by establishing water-mediated hydrogen bonds between the 2-amino group and Q162
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additional information
?
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6-fluoroanthraniloyl-AMP (6FABA-AMP), an inhibitor of PQS biosynthesis, is a good substrate of enzyme PqsA, enzyme binding structure analysis of 6-fluoroanthraniloyl-AMP and anthraniloyl-AMP, overview. 6FABA-AMP binds to PqsANTD in a similar way to anthraniloyl-AMP, by establishing water-mediated hydrogen bonds between the 2-amino group and Q162
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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
ATP + anthranilate + CoA
AMP + diphosphate + anthraniloyl-CoA
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-
-
?
ATP + anthranilate + CoA
AMP + diphosphate + anthranilyl-CoA
the Pseudomonas quinolone signal PQS is a 3-hydroxy-4-quinolone with a 2-alkyl substitution, which is synthesized by the condensation of anthranilic acid with a 3-keto-fatty acid, pathway for PQS biosynthesis, anthranilate is activated by PqsA to form anthraniloyl-CoA, and this is condensed with 2-oxo-decanoyl-ACP which is recruited from the fatty acid biosynthetic pathway, overview
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
effects of substrate analogues on in vitro anthranilate-CoA ligase activity and in vivo PQS production in Pseudomonas aeruginosa, overview
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additional information
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effects of substrate analogues on in vitro anthranilate-CoA ligase activity and in vivo PQS production in Pseudomonas aeruginosa, overview
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
PqsA belongs to the ANL superfamily of anthranilate-CoA ligases that recognize the amino group of anthranilate through a water-mediated hydrogen bond
metabolism
the enzyme performs substrate activation in Pseudomonas aeruginosa quinolone signal (PQS) biosynthesis
physiological function
the enzyme performs substrate activation in Pseudomonas aeruginosa quinolone signal (PQS) biosynthesis
additional information
additional information
active site structure and structure comparisons, overview. In PqsANTD, the 2-amino group of the anthraniloyl moiety is hydrogen-bonded to a conserved water molecule, which is coordinated by the side chain of Q162 and the carbonyl oxygen atom of G307. Q162 is located directly adjacent to the P-loop
additional information
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active site structure and structure comparisons, overview. In PqsANTD, the 2-amino group of the anthraniloyl moiety is hydrogen-bonded to a conserved water molecule, which is coordinated by the side chain of Q162 and the carbonyl oxygen atom of G307. Q162 is located directly adjacent to the P-loop
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
The two half-reactions are cooperatively catalyzed by a large N-terminal domain and a smaller C-terminal domain separated by a flexible linker, the latter undergoes large conformational rearrangements in the course of the catalytic cycle. In PqsA, the adenine ring of the complexed adenylate moiety is sandwiched between the main-chain atoms of G279, S280, and P281 from a loop between beta12 and alpha12 on one side and the side chain of I301 on the opposite side, structure analysis, overview
additional information
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The two half-reactions are cooperatively catalyzed by a large N-terminal domain and a smaller C-terminal domain separated by a flexible linker, the latter undergoes large conformational rearrangements in the course of the catalytic cycle. In PqsA, the adenine ring of the complexed adenylate moiety is sandwiched between the main-chain atoms of G279, S280, and P281 from a loop between beta12 and alpha12 on one side and the side chain of I301 on the opposite side, structure analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified isolated N-terminal domain of anthranilate-CoA ligase PqsA in complex with anthraniloyl- and 6-fluoroanthraniloyl-AMP, sitting drop vapor diffusion technique, mixing of 200 nl of protein solution with 200 nl of reservoir solution containing 0.1 M Na3 citrate, pH 5.8-6.3, 22-28% w/v PEG 3350, and 0.2-0.5 M NH4OAc. Crystals can only be obtained in the presence of substrates, leading to complexes with anthraniloyl-AMP or 6-fluoroanthraniloyl-AMP, 20°C, X-ray diffraction structure determination and analysis at 1.43-1.90 A resolution, molecular replacement using the structure of the benzoate-CoA ligase from Bacillus xenoverans LB400, PDB ID 2V7B, as a search model, modeling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged PqsA 58fold from Escherichia coli by ammonium sulfate fractionation, metal affinity and hydrophobic interaction chromatography, and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pqsA is part of the pqsABCDE operon, sequence comparisons, expression of the His-tagged enzyme in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme might be an attractive target for anti-infective agents
synthesis
three anthranilate derivatives, N-methylanthranilate, methyl anthranilate, and methyl N-methylanthranilate are synthesized using metabolically engineered stains of Escherichia coli. NMT encoding N-methyltransferase from Ruta graveolens, AMAT encoding anthraniloyl-coenzyme A (CoA):methanol acyltransferase from Vitis labrusca, and pqsA encoding anthranilate coenzyme A ligase from Pseudomonas aeruginosa are cloned and Eschetrichia coli strains harboring these genes were used to synthesize the three desired compounds. Escherichia coli mutants (metJ, trpD, tyrR mutants), which provide more anthranilate and/or S-adenosyl methionine, are used to increase the production of the synthesized compounds. 0.1853 mM N-methylanthranilate and 0.0952 mM methyl N-methylanthranilate are synthesized
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Coleman, J.P.; Hudson, L.L.; McKnight, S.L.; Farrow, J.M.; Calfee, M.W.; Lindsey, C.A.; Pesci, E.C.
Pseudomonas aeruginosa PqsA is an anthranilate-coenzyme A ligase
J. Bacteriol.
190
1247-1255
2008
Pseudomonas aeruginosa (Q9I4X3), Pseudomonas aeruginosa
Witzgall, F.; Ewert, W.; Blankenfeldt, W.
Structures of the N-terminal domain of PqsA in complex with anthraniloyl- and 6-fluoroanthraniloyl-AMP substrate activation in Pseudomonas quinolone signal (PQS) biosynthesis
ChemBioChem
18
2045-2055
2017
Pseudomonas aeruginosa (Q9I4X3), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q9I4X3)
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