pqsL, a putative FAD-dependent monooxygenase,  is responsible for  the N-oxidation in  2-alkyl quinolones (HHQ) and 4-hydroxy quinolones (PQS), the molecules accountable for the quorum sensing cross talk between opportunistic  pathogens Psuedomonas aeruginosa and Burkholderia thialandesis. Through the in vitro and in vivo enzymology and spectroscopic assays, the aim is to ascertain the enzymatic activity of pqsL and the biosynthetic pathway of N-oxide quinolones. Our studies have shown that the production of N-oxides occurs in the presence of pqsL through FAD reduction.  Interestingly, the feeding studies of pqsL with various HHQ and PQS molecules showed neither FAD reduction nor production of any N-oxides. This suggests that biosynthesis of these N-oxides do not occur through the HHQ or PQS. Furthermore, the in vitro enzymatic assay of pqsL with various substrates showed a variety of amino-substituted substrates to be the precursors of the biosynthesis of N-oxides

Ascertaining the enzymatic activity of pqsL and the biosynthetic pathway of N-oxide quinolone molecules

244th National Meeting (2012)

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