EC - Anthraniloyl-CoA anthraniloyltransferase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
anthraniloyl-CoA anthraniloyltransferase
Other name:
pqsD (gene name)
Systematic name:
anthraniloyl-CoA:malonyl-CoA anthraniloyltransferase



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, 2-aminobenzoylacetyl-CoA thioesterase, is present, it removes the CoA moiety from the product, forming the stable 2-aminobenzoylacetate.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Bera, A. K., Atanasova, V., Robinson, H., Eisenstein, E., Coleman, J. P., Pesci, E. C., Parsons, J. F.
    Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate.
    Biochemistry 48: 8644-8655 (2009). [PMID: 19694421]
  2. Dulcey, C. E., Dekimpe, V., Fauvelle, D. A., Milot, S., Groleau, M. C., Doucet, N., Rahme, L. G., Lepine, F., 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: 1481-1491 (2013). [PMID: 24239007]
  3. Drees, S. L., Fetzner, S.
    PqsE of Pseudomonas aeruginosa Acts as Pathway-Specific Thioesterase in the Biosynthesis of Alkylquinolone Signaling Molecules.
    Chem. Biol. 22: 611-618 (2015). [PMID: 25960261]

[EC created 2017]