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Literature summary extracted from

  • 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 (2009), Biochemistry, 48, 8644-8655.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.230 overexpression in Escherichia coli Pseudomonas aeruginosa
2.3.1.262 expression in Escherichia coli Pseudomonas aeruginosa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.230 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 Pseudomonas aeruginosa
2.3.1.262 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 Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.230 C112A the C112A mutant is inactive although it still reversibly binds anthraniloyl-CoA Pseudomonas aeruginosa
2.3.1.262 C112A mutant is inactive although it still reversibly binds anthraniloyl-CoA Pseudomonas aeruginosa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.230 36000
-
 2 * 36000 Pseudomonas aeruginosa
2.3.1.230 72800
-
 gel filtration, laser light scattering Pseudomonas aeruginosa
2.3.1.262 72800
-
 gel filtration Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.230 malonyl-CoA + 2-aminobenzoyl-CoA Pseudomonas aeruginosa 2-aminobenzoyl-CoA i.e. anthraniloyl-CoA 2 CoA + 4-hydroxy-2(1H)-quinolone + CO2 i.e. 2,4-dihydroxyquinoline ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.230 Pseudomonas aeruginosa P20582
-
-
2.3.1.262 Pseudomonas aeruginosa P20582 cf. EC 2.3.1.230
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.230
-
 Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.230 malonyl-CoA + 2-aminobenzoyl-CoA 2-aminobenzoyl-CoA i.e. anthraniloyl-CoA Pseudomonas aeruginosa 2 CoA + 4-hydroxy-2(1H)-quinolone + CO2 i.e. 2,4-dihydroxyquinoline ?
2.3.1.262 anthraniloyl-CoA + malonyl-CoA
-
 Pseudomonas aeruginosa 2,4-dihydroxyquinoline + 2 CoA + CO2 + ? in vitro overall reaction ?

Subunits

EC Number Subunits Comment Organism
2.3.1.230 homodimer 2 * 36000 Pseudomonas aeruginosa
2.3.1.262 dimer 2 * 36379, calculated Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
2.3.1.230 PqsD
-
 Pseudomonas aeruginosa
2.3.1.262 PqsD
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.230 37
-
 assay at Pseudomonas aeruginosa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.262 0.3
-
 anthraniloyl-CoA pH 7.5, 37°C Pseudomonas aeruginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.230 7.5
-
 assay at Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
2.3.1.230 physiological function PqsD is a quinolone signal biosynthetic enzyme Pseudomonas aeruginosa