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-aminobenzoyl)acetate [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
PAEPA0997(pqsB) PA0998(pqsC)
PAEVN297_1030 N297_1031
PAEIN296_1030 N296_1031
PAUPA14_51410(pqsC) PA14_51420(pqsB)
PAPPSPA7_4400 PSPA7_4401
PAGPLES_43271(pqsC) PLES_43281(pqsB)
PAFPAM18_4050(pqsC) PAM18_4051(pqsB)
PNCNCGM2_1851(pqsB) NCGM2_1852(pqsC)
PAEBNCGM1900_1670(pqsC) NCGM1900_1671(pqsB)
PDKPADK2_20750 PADK2_20755
PSGG655_20310 G655_20315
PRPM062_05435 M062_05440
PAEPPA1S_20980 PA1S_20985
PAERPA1R_gp4594 PA1R_gp4595
PAEMU769_20825 U769_20830
PAELT223_22105 T223_22110
PAESSCV20265_4444 SCV20265_4445
PAEUBN889_01049(pqsB) BN889_01050(pqsC)
PAEGAI22_12955 AI22_12960
PAECM802_1027 M802_1028
PAEOM801_1030 M801_1031
SECHB18_16615 B18_16620
 » 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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