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Literature summary extracted from

  • Steinbach, A.; Maurer, C.K.; Weidel, E.; Henn, C.; Brengel, C.; Hartmann, R.W.; Negri, M.
    Molecular basis of HHQ biosynthesis: molecular dynamics simulations, enzyme kinetic and surface plasmon resonance studies (2013), BMC Biophys., 6, 10.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.230 S317F inactive mutant enzyme Pseudomonas aeruginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.230 0.875
-
 2-aminobenzoyl-CoA pH 7, 37°C Pseudomonas aeruginosa
2.3.1.230 1.3
-
 3-oxodecanoate pH 7, 37°C 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. The enzyme is involved in the biosynthesis of the Pseudomonas Quinolone Signal 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
-
-
-

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 3-oxodecanoate + 2-aminobenzoyl-CoA
-
 Pseudomonas aeruginosa CoA + 2-heptyl-4-hydroxyquinoline + CO2 + H2O
-
 ?
2.3.1.230 malonyl-CoA + 2-aminobenzoyl-CoA 2-aminobenzoyl-CoA i.e. anthraniloyl-CoA. The enzyme is involved in the biosynthesis of the Pseudomonas Quinolone Signal Pseudomonas aeruginosa 2 CoA + 4-hydroxy-2(1H)-quinolone + CO2 i.e. 2,4-dihydroxyquinoline ?
2.3.1.230 malonyl-CoA + 2-aminobenzoyl-CoA 2-aminobenzoyl-CoA i.e. anthraniloyl-CoA. Ping-pong mechanism for PqsD with 2-aminobenzoyl-CoA as first substrate. Trajectory analysis of different PqsD complexes evidences ligand-dependent induced-fit motions affecting the modified 2-aminobenzoyl-CoA funnel access to the exposure of a secondary channel. A tunnel-network is formed in which Ser317 plays an important role by binding to both substrates Pseudomonas aeruginosa 2 CoA + 4-hydroxy-2(1H)-quinolone + CO2 i.e. 2,4-dihydroxyquinoline ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.230 0.0165
-
 2-aminobenzoyl-CoA pH 7, 37°C Pseudomonas aeruginosa
2.3.1.230 0.0165
-
 3-oxodecanoate pH 7, 37°C Pseudomonas aeruginosa