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1.14.13.182

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

References:

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 1.14.13.182 created 2013]

2.3.1.230

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, PDB

References:

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 2.3.1.230 created 2013, modified 2017]

3.1.2.32

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, PDB

References:

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 3.1.2.32 created 2016]