The Enzyme Database

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Accepted name: 2-heptyl-3-hydroxy-4(1H)-quinolone synthase
Reaction: 2-heptyl-4(1H)-quinolone + NADH + H+ + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
Glossary: 2-heptyl-4(1H)-quinolone = 2-heptyl-4-hydroxyquinoline
2-heptyl-3-hydroxy-4(1H)-quinolone = 2-heptyl-3,4-dihydroxyquinoline
Other name(s): PqsH; 2-heptyl-3,4-dihydroxyquinoline synthase
Systematic name: 2-heptyl-4(1H)-quinolone,NADH:oxygen oxidoreductase (3-hydroxylating)
Comments: The enzyme from the bacterium Pseudomonas aeruginosa catalyses the terminal step in biosynthesis of the signal molecule 2-heptyl-3,4-dihydroxyquinoline that plays a role in regulation of virulence genes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Schertzer, J.W., Brown, S.A. and Whiteley, M. Oxygen levels rapidly modulate Pseudomonas aeruginosa social behaviours via substrate limitation of PqsH. Mol. Microbiol. 77 (2010) 1527–1538. [DOI] [PMID: 20662781]
[EC created 2013]
Accepted name: 2-heptyl-4(1H)-quinolone synthase
Reaction: octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O (overall reaction)
(1a) octanoyl-CoA + L-cysteinyl-[PqsC protein] = S-octanoyl-L-cysteinyl-[PqsC protein] + CoA
(1b) S-octanoyl-L-cysteinyl-[PqsC protein] + (2-aminobenzoyl)acetate = 1-(2-aminophenyl)decane-1,3-dione + CO2 + L-cysteinyl-[PqsC protein]
(1c) 1-(2-aminophenyl)decane-1,3-dione = 2-heptyl-4-quinolone + H2O
Glossary: 2-heptyl-4-quinolone = 2-heptylquinolin-4(1H)-one
Other name(s): pqsBC (gene names); malonyl-CoA:anthraniloyl-CoA C-acetyltransferase (decarboxylating)
Systematic name: octanoyl-CoA:(2-aminobenzoyl)acetate octanoyltransferase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is a heterodimeric complex. The PqsC subunit acquires an octanoyl group from octanoyl-CoA and attaches it to an internal cysteine residue. Together with the PqsB subunit, the proteins catalyse the coupling of the octanoyl group with (2-aminobenzoyl)acetate, leading to decarboxylation and dehydration events that result in closure of the quinoline ring.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Dulcey, C.E., Dekimpe, V., Fauvelle, D.A., Milot, S., Groleau, M.C., Doucet, N., Rahme, L.G., Lepine, F. and Deziel, E. The end of an old hypothesis: the pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. Chem. Biol. 20 (2013) 1481–1491. [DOI] [PMID: 24239007]
2.  Drees, S.L., Li, C., Prasetya, F., Saleem, M., Dreveny, I., Williams, P., Hennecke, U., Emsley, J. and Fetzner, S. PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism. J. Biol. Chem. 291 (2016) 6610–6624. [DOI] [PMID: 26811339]
[EC created 2013, modified 2017]
Accepted name: 2-aminobenzoylacetyl-CoA thioesterase
Reaction: (2-aminobenzoyl)acetyl-CoA + H2O = (2-aminobenzoyl)acetate + CoA
Other name(s): pqsE (gene name)
Systematic name: (2-aminobenzoyl)acetyl-CoA hydrolase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the production of the signal molecule 2-heptyl-4(1H)-quinolone (HHQ).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Yu, S., Jensen, V., Seeliger, J., Feldmann, I., Weber, S., Schleicher, E., Haussler, S. and Blankenfeldt, W. Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein. Biochemistry 48 (2009) 10298–10307. [DOI] [PMID: 19788310]
2.  Drees, S.L. and Fetzner, S. PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules. Chem. Biol. 22 (2015) 611–618. [DOI] [PMID: 25960261]
[EC created 2016]

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