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Literature summary extracted from

  • Drees, S.L.; Ernst, S.; Belviso, B.D.; Jagmann, N.; Hennecke, U.; Fetzner, S.
    PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa (2018), J. Biol. Chem., 293, 9345-9357 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.B14 analysis of the PqsL structure (PDB ID 2X3N), which has been solved to a resolution of 1.75 A and remodeling of a loop region, which aligns with a loop reported to be involved in NADPH and FAD binding in pHBH, comparison to the structure of pHBH of Pseudomonas fluorescens (PDB code 1PBE), structure-function analysis, detailed overview. The conformation found in PqsL is closer to the open state, which is rather unusual for a group A monooxygenase without substrate bound. The enzyme is not capable of binding NAD(P)H in the alleged mode because several of the crucial positions are replaced by dysfunctional substitutions Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.B14 additional information in vitro reconstitution of the PqsL/PqsBC reaction is feasible by using the FAD reductase HpaC, the AQ:AQNO ratio is increased in an hpaC-deletion mutant of Pseudomonas aeruginosa strain PAO1 compared with the ratio in the wild-type strain Pseudomonas aeruginosa

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.B14 additional information product inhibition of PqsL is possible Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2 Pseudomonas aeruginosa
-
2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2 Pseudomonas aeruginosa ATCC 15692
-
2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2 Pseudomonas aeruginosa 1C
-
2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2 Pseudomonas aeruginosa PRS 101
-
2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2 Pseudomonas aeruginosa DSM 22644
-
2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2 Pseudomonas aeruginosa CIP 104116
-
2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2 Pseudomonas aeruginosa LMG 12228
-
2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2 Pseudomonas aeruginosa JCM 14847
-
2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 additional information Pseudomonas aeruginosa PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa ?
-
-
1.14.14.B14 additional information Pseudomonas aeruginosa ATCC 15692 PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa ?
-
-
1.14.14.B14 additional information Pseudomonas aeruginosa 1C PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa ?
-
-
1.14.14.B14 additional information Pseudomonas aeruginosa PRS 101 PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa ?
-
-
1.14.14.B14 additional information Pseudomonas aeruginosa DSM 22644 PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa ?
-
-
1.14.14.B14 additional information Pseudomonas aeruginosa CIP 104116 PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa ?
-
-
1.14.14.B14 additional information Pseudomonas aeruginosa LMG 12228 PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa ?
-
-
1.14.14.B14 additional information Pseudomonas aeruginosa JCM 14847 PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa ?
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.B14 Pseudomonas aeruginosa Q9HWJ1
-
-
1.14.14.B14 Pseudomonas aeruginosa 1C Q9HWJ1
-
-
1.14.14.B14 Pseudomonas aeruginosa ATCC 15692 Q9HWJ1
-
-
1.14.14.B14 Pseudomonas aeruginosa CIP 104116 Q9HWJ1
-
-
1.14.14.B14 Pseudomonas aeruginosa DSM 22644 Q9HWJ1
-
-
1.14.14.B14 Pseudomonas aeruginosa JCM 14847 Q9HWJ1
-
-
1.14.14.B14 Pseudomonas aeruginosa LMG 12228 Q9HWJ1
-
-
1.14.14.B14 Pseudomonas aeruginosa PRS 101 Q9HWJ1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2
-
Pseudomonas aeruginosa 2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2
-
Pseudomonas aeruginosa ATCC 15692 2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2
-
Pseudomonas aeruginosa 1C 2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2
-
Pseudomonas aeruginosa PRS 101 2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2
-
Pseudomonas aeruginosa DSM 22644 2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2
-
Pseudomonas aeruginosa CIP 104116 2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2
-
Pseudomonas aeruginosa LMG 12228 2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 2-aminobenzoylacetate + FADH2 + O2
-
Pseudomonas aeruginosa JCM 14847 2-hydroxylaminobenzoylacetate + FAD + H2O
-
?
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa Pseudomonas aeruginosa ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa, product identification by LC-MS. FAD reductase HpaC (UniProt Q9HWT6) supports PqsL activity in the coupled PqsL/PqsBC assay Pseudomonas aeruginosa ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa Pseudomonas aeruginosa ATCC 15692 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa, product identification by LC-MS. FAD reductase HpaC (UniProt Q9HWT6) supports PqsL activity in the coupled PqsL/PqsBC assay Pseudomonas aeruginosa ATCC 15692 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa Pseudomonas aeruginosa 1C ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa, product identification by LC-MS. FAD reductase HpaC (UniProt Q9HWT6) supports PqsL activity in the coupled PqsL/PqsBC assay Pseudomonas aeruginosa 1C ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa Pseudomonas aeruginosa PRS 101 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa, product identification by LC-MS. FAD reductase HpaC (UniProt Q9HWT6) supports PqsL activity in the coupled PqsL/PqsBC assay Pseudomonas aeruginosa PRS 101 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa Pseudomonas aeruginosa DSM 22644 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa, product identification by LC-MS. FAD reductase HpaC (UniProt Q9HWT6) supports PqsL activity in the coupled PqsL/PqsBC assay Pseudomonas aeruginosa DSM 22644 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa Pseudomonas aeruginosa CIP 104116 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa, product identification by LC-MS. FAD reductase HpaC (UniProt Q9HWT6) supports PqsL activity in the coupled PqsL/PqsBC assay Pseudomonas aeruginosa CIP 104116 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa Pseudomonas aeruginosa LMG 12228 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa, product identification by LC-MS. FAD reductase HpaC (UniProt Q9HWT6) supports PqsL activity in the coupled PqsL/PqsBC assay Pseudomonas aeruginosa LMG 12228 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa Pseudomonas aeruginosa JCM 14847 ?
-
-
1.14.14.B14 additional information PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa, product identification by LC-MS. FAD reductase HpaC (UniProt Q9HWT6) supports PqsL activity in the coupled PqsL/PqsBC assay Pseudomonas aeruginosa JCM 14847 ?
-
-

Synonyms

EC Number Synonyms Comment Organism
1.14.14.B14 PA4190
-
Pseudomonas aeruginosa
1.14.14.B14 PqsL
-
Pseudomonas aeruginosa

Temperature Optimum [┬░C]

EC Number Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
1.14.14.B14 30 37 assay at Pseudomonas aeruginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.14.B14 7.3 9.5 assay at Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.B14 FAD the Redox potential of PqsL is sufficiently positive for direct reduction by free flavin, determination of a two-electron midpoint potential of -140 mV for the PqsL-internal FAD Pseudomonas aeruginosa
1.14.14.B14 FMN
-
Pseudomonas aeruginosa
1.14.14.B14 additional information PqsL is able to receive electrons from reduced FAD. Alternatively, PqsL might exchange its internal FAD cofactor for FADH2, but because the reaction can be supported by reduced FMN as well (albeit with lower efficiency), a cofactor exchange is rather unlikely. PqsL depends on free reduced flavin as electron donor instead of NAD(P)H. The enzyme is not capable of binding NAD(P)H in the alleged mode because several of the crucial positions are replaced by dysfunctional substitutions Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
1.14.14.B14 evolution enzyme PqsL belongs to the class A flavoprotein monooxygenases Pseudomonas aeruginosa
1.14.14.B14 metabolism 2-alkyl-4-hydroxyquinoline-N-oxide (AQNO) biosynthesis involves the enzymes encoded by the pqsABCDE operon, which mediate 2-alkyl-4-hydroxyquinoline biosynthesis from anthranilic acid and activated fatty acids, and additionally requires PqsL, a putative flavin-dependent monooxygenase encoded by a presumably monocistronic gene. AQNO biosynthesis branches off from 2-ABA or an immediate downstream intermediate. Biosynthesis of alkyl quinolones in Pseudomonas aeruginosa and possible reactions for 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO) synthesis. FAD reductase HpaC supports PqsL activity in the coupled PqsL/PqsBC assay. Deletion of hpaC in Pseudomonas aeruginosa strain PAO1 influences the HQNO to HHQ ratio Pseudomonas aeruginosa
1.14.14.B14 additional information PqsL structurally resembles class A flavoprotein monooxygenases such as p-hydroxybenzoate 3-hydroxylase (pHBH, EC 1.14.13.2) and 3-hydroxybenzoate 6-hydroxylase (EC 1.14.13.24). But unlike related enzymes, PqsL hydroxylates a primary aromatic amine group, and it does not use NAD(P)H as cosubstrate, but unexpectedly requires reduced flavin as electron donor. A structural comparison with pHBH, the model enzyme of class A flavoprotein monooxygenases, reveals that structural features associated with NAD(P)H binding are missing in PqsL Pseudomonas aeruginosa
1.14.14.B14 physiological function alkyl hydroxyquinoline N-oxides (AQNOs) are antibiotic compounds produced by the opportunistic bacterial pathogen Pseudomonas aeruginosa. They are products of the alkyl quinolone (AQ) biosynthetic pathway, which also generates the quorum-sensing molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS). PqsL is the key enzyme for AQNO production. PqsL is active toward 2-aminobenzoylacetate (2-ABA), the central intermediate of the AQ pathway, and forms the unstable compound 2-hydroxylaminobenzoylacetate, which is preferred over 2-ABA as a substrate of the downstream enzyme PqsBC. Although 2-heptyl-3-hydroxy-4(1H)-quinolone (Pseudomonas quinolone signal, PQS) and its immediate biosynthetic precursor 2-heptyl-4(1H)-quinolone (HHQ) mainly serve as quorum sensing signals, contributing to the control of virulence gene expression, 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO) acts as a toxin against both microorganisms and eukaryotic cells. PqsL is the key enzyme for biosynthesis of HQNO, it catalyzes the N-oxidation of a biosynthetic precursor molecule other than HHQ Pseudomonas aeruginosa