KEGG   ENZYME: 2.3.1.262Help
Entry
EC 2.3.1.262                Enzyme                                 

Name
anthraniloyl-CoA anthraniloyltransferase;
pqsD (gene name)
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
BRITE hierarchy
Sysname
anthraniloyl-CoA:malonyl-CoA anthraniloyltransferase
Reaction(IUBMB)
anthraniloyl-CoA + malonyl-CoA = 2-aminobenzoylacetyl-CoA + CoA + CO2 (overall reaction) [RN:R11588];
(1a) anthraniloyl-CoA + L-cysteinyl-[PqsD protein] = S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA [RN:R11586];
(1b) S-anthraniloyl-L-cysteinyl-[PqsD protein] + malonyl-CoA = 2-aminobenzoylacetyl-CoA + CO2 + L-cysteinyl-[PqsD protein] [RN:R11587]
Reaction(KEGG)
Substrate
anthraniloyl-CoA [CPD:C02247];
malonyl-CoA [CPD:C00083];
L-cysteinyl-[PqsD protein];
S-anthraniloyl-L-cysteinyl-[PqsD protein]
Product
2-aminobenzoylacetyl-CoA [CPD:C21452];
CoA [CPD:C00010];
CO2 [CPD:C00011];
S-anthraniloyl-L-cysteinyl-[PqsD protein];
L-cysteinyl-[PqsD protein]
Comment
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the synthesis of the secondary metabolites 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone. The enzyme transfers an anthraniloyl group from anthraniloyl-CoA to an internal L-cysteine residue, followed by its transfer to malonyl-CoA to produce a short-lived product that can cyclize spontaneously to form 4-hydroxy-2(1H)-quinolone. However, when EC 3.1.2.32, 2-aminobenzoylacetyl-CoA thioesterase, is present, it removes the CoA moiety from the product, forming the stable 2-aminobenzoylacetate.
History
EC 2.3.1.262 created 2017
Pathway
ec00405  Phenazine biosynthesis
ec01130  Biosynthesis of antibiotics
Orthology
K18003  anthraniloyl-CoA anthraniloyltransferase
Genes
PAE: PA0999(pqsD)
PAEV: N297_1032(pqsD)
PAEI: N296_1032(pqsD)
PAU: PA14_51390(pqsD)
PAP: PSPA7_4399(fabH1)
PAG: PLES_43261(pqsD)
PAF: PAM18_4049(pqsD)
PNC: NCGM2_1853(pqsD)
PAEB: NCGM1900_1669(pqsD)
PDK: PADK2_20745
PAEP: PA1S_20975
PAEM: U769_20820
PAEL: T223_22100
PAEU: BN889_01051(pqsD)
PAEG: AI22_12965
PAEC: M802_1029(pqsD)
PAEO: M801_1032(pqsD)
 » show all
Taxonomy
Reference
1  [PMID:19694421]
  Authors
Bera AK, Atanasova V, Robinson H, Eisenstein E, Coleman JP, Pesci EC, Parsons JF
  Title
Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate.
  Journal
Biochemistry 48:8644-55 (2009)
DOI:10.1021/bi9009055
  Sequence
[pae:PA0999]
Reference
2  [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
3  [PMID:25960261]
  Authors
Drees SL, Fetzner S
  Title
PqsE of Pseudomonas aeruginosa Acts as Pathway-Specific Thioesterase in the Biosynthesis of Alkylquinolone Signaling Molecules.
  Journal
Chem Biol 22:611-8 (2015)
DOI:10.1016/j.chembiol.2015.04.012
Other DBs
ExplorEnz - The Enzyme Database: 2.3.1.262
IUBMB Enzyme Nomenclature: 2.3.1.262
ExPASy - ENZYME nomenclature database: 2.3.1.262
BRENDA, the Enzyme Database: 2.3.1.262

DBGET integrated database retrieval system