KEGG   ENZYME: 2.3.1.230
Entry
EC 2.3.1.230                Enzyme                                 

Name
2-heptyl-4(1H)-quinolone synthase;
pqsBC (gene names);
malonyl-CoA:anthraniloyl-CoA C-acetyltransferase (decarboxylating)
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
Sysname
octanoyl-CoA:(2-aminobenzoyl)acetate octanoyltransferase
Reaction(IUBMB)
octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O (overall reaction) [RN:R10589];
(1a) octanoyl-CoA + L-cysteinyl-[PqsC protein] = S-octanoyl-L-cysteinyl-[PqsC protein] + CoA [RN:R10590];
(1b) S-octanoyl-L-cysteinyl-[PqsC protein] + (2-aminobenzoyl)acetate = 1-(2-aminophenyl)decane-1,3-dione + CO2 + L-cysteinyl-[PqsC protein] [RN:R11589];
(1c) 1-(2-aminophenyl)decane-1,3-dione = 2-heptyl-4-quinolone + H2O [RN:R11590]
Reaction(KEGG)
Substrate
octanoyl-CoA [CPD:C01944];
2-aminobenzoylacetate [CPD:C21453];
L-cysteinyl-[PqsC protein];
S-octanoyl-L-cysteinyl-[PqsC protein];
1-(2-aminophenyl)decane-1,3-dione [CPD:C21490]
Product
2-heptyl-4-quinolone [CPD:C20643];
CoA [CPD:C00010];
CO2 [CPD:C00011];
H2O [CPD:C00001];
S-octanoyl-L-cysteinyl-[PqsC protein];
1-(2-aminophenyl)decane-1,3-dione [CPD:C21490];
L-cysteinyl-[PqsC protein]
Comment
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.
History
EC 2.3.1.230 created 2013, modified 2017
Pathway
ec00405  Phenazine biosynthesis
ec01110  Biosynthesis of secondary metabolites
Orthology
K18001  2-heptyl-4(1H)-quinolone synthase subunit PqsB
K18002  2-heptyl-4(1H)-quinolone synthase subunit PqsC
Genes
PAE: PA0997(pqsB) PA0998(pqsC)
PAEV: N297_1030 N297_1031
PAEI: N296_1030 N296_1031
PAU: PA14_51410(pqsC) PA14_51420(pqsB)
PAP: PSPA7_4400 PSPA7_4401
PAG: PLES_43271(pqsC) PLES_43281(pqsB)
PAF: PAM18_4050(pqsC) PAM18_4051(pqsB)
PNC: NCGM2_1851(pqsB) NCGM2_1852(pqsC)
PAEB: NCGM1900_1670(pqsC) NCGM1900_1671(pqsB)
PDK: PADK2_20750 PADK2_20755
PAEU: BN889_01049(pqsB) BN889_01050(pqsC)
 » show all
Reference
1  [PMID:24239007]
  Authors
Dulcey CE, Dekimpe V, Fauvelle DA, Milot S, Groleau MC, Doucet N, Rahme LG, Lepine F, Deziel E
  Title
The end of an old hypothesis: the pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids.
  Journal
Chem Biol 20:1481-91 (2013)
DOI:10.1016/j.chembiol.2013.09.021
Reference
2  [PMID:26811339]
  Authors
Drees SL, Li C, Prasetya F, Saleem M, Dreveny I, Williams P, Hennecke U, Emsley J, Fetzner S
  Title
PqsBC, a Condensing Enzyme in the Biosynthesis of the Pseudomonas aeruginosa Quinolone Signal: CRYSTAL STRUCTURE, INHIBITION, AND REACTION MECHANISM.
  Journal
J Biol Chem 291:6610-24 (2016)
DOI:10.1074/jbc.M115.708453
  Sequence
[pae:PA0998]
Other DBs
ExplorEnz - The Enzyme Database: 2.3.1.230
IUBMB Enzyme Nomenclature: 2.3.1.230
ExPASy - ENZYME nomenclature database: 2.3.1.230
BRENDA, the Enzyme Database: 2.3.1.230
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