ATP + anthranilate + CoA = AMP + diphosphate + anthraniloyl-CoA
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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
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
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
isoenzyme E2 is induced anaerobically by 2-aminobenzoate and plays a role in anaerobic metabolism, E3 is induced aerobically by 2-aminobenzoate and is a key enzyme of aerobic metabolism
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
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
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
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
isoenzyme E2 is induced anaerobically by 2-aminobenzoate and plays a role in anaerobic metabolism, E3 is induced aerobically by 2-aminobenzoate and is a key enzyme of aerobic metabolism
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
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
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
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
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
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
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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
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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
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
Anaerobic degradation of 2-aminobenzoic acid (anthranilic acid) via benzoyl-coenzyme A (CoA) and cyclohex-1-enecarboxyl-CoA in a denitrifying bacterium
Structures of the N-terminal domain of PqsA in complex with anthraniloyl- and 6-fluoroanthraniloyl-AMP substrate activation in Pseudomonas quinolone signal (PQS) biosynthesis