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March 25, 2016

Volume 291Issue 13p6610-7220
Open Access
On The Cover: PqsBC of Pseudomonas aeruginosa is a FabH-like condensing enzyme with a unique heterodimeric structure. It catalyzes the formation of the quorum sensing signal molecule 2-heptyl-4(1H)-quinolone from octanoyl-coenzyme A and 2-aminobenzoylacetate. PqsBC is inhibited by 2-aminoacetophenone, a major side product of the biosynthetic pathway. The fluorescence change of 2-aminoacetophenone upon binding to PqsBC enabled its use as a mechanistic probe. For details see the article by Drees et al., pages 6610–6624....
On The Cover: PqsBC of Pseudomonas aeruginosa is a FabH-like condensing enzyme with a unique heterodimeric structure. It catalyzes the formation of the quorum sensing signal molecule 2-heptyl-4(1H)-quinolone from octanoyl-coenzyme A and 2-aminobenzoylacetate. PqsBC is inhibited by 2-aminoacetophenone, a major side product of the biosynthetic pathway. The fluorescence change of 2-aminoacetophenone upon binding to PqsBC enabled its use as a mechanistic probe. For details see the article by Drees et al., pages 6610–6624.

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