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Literature summary extracted from

  • 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 (2017), ChemBioChem, 18, 2045-2055 .
    View publication on PubMed

Application

EC Number Application Comment Organism
6.2.1.32 drug development the enzyme might be an attractive target for anti-infective agents Pseudomonas aeruginosa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.2.1.32 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 Pseudomonas aeruginosa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.32 Mg2+ required Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.32 ATP + anthranilate + CoA Pseudomonas aeruginosa
-
 AMP + diphosphate + anthraniloyl-CoA
-
 ?
6.2.1.32 ATP + anthranilate + CoA Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
 AMP + diphosphate + anthraniloyl-CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.32 Pseudomonas aeruginosa Q9I4X3
-
-
6.2.1.32 Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 Q9I4X3
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.2.1.32 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 Pseudomonas aeruginosa
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.32 ATP + anthranilate + CoA
-
 Pseudomonas aeruginosa AMP + diphosphate + anthraniloyl-CoA
-
 ?
6.2.1.32 ATP + anthranilate + CoA
-
 Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 AMP + diphosphate + anthraniloyl-CoA
-
 ?
6.2.1.32 additional information 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 Pseudomonas aeruginosa ?
-
 ?
6.2.1.32 additional information 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 Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.2.1.32 More 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 Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
6.2.1.32 anthranilate-CoA ligase
-
 Pseudomonas aeruginosa
6.2.1.32 PqsA
-
 Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.32 ATP
-
 Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
6.2.1.32 evolution PqsA belongs to the ANL superfamily of anthranilate-CoA ligases that recognize the amino group of anthranilate through a water-mediated hydrogen bond Pseudomonas aeruginosa
6.2.1.32 metabolism the enzyme performs substrate activation in Pseudomonas aeruginosa quinolone signal (PQS) biosynthesis Pseudomonas aeruginosa
6.2.1.32 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 Pseudomonas aeruginosa
6.2.1.32 physiological function the enzyme performs substrate activation in Pseudomonas aeruginosa quinolone signal (PQS) biosynthesis Pseudomonas aeruginosa