S-ribosylhomocysteine lyase (LuxS)

S-ribosylhomocysteine lyase (LuxS) is an iron-dependent metalloenzyme (EC 4.4.1.21) found in many bacteria that cleaves S-ribosylhomocysteine to produce L-homocysteine and 4,5-dihydroxy-2,3-pentanedione (DPD), the precursor of the universal bacterial signaling molecule autoinducer-2 (AI-2)[1][2][4][7]. LuxS plays a key role in bacterial quorum sensing, a system of cell communication based on cell density that regulates biofilm formation, virulence, antibiotic resistance, and other group behaviors. It is highly conserved and encoded by the luxS gene in most bacteria[1][2][7]. LuxS belongs to the carbon-sulfur lyase class and requires a metal cofactor, commonly Fe2+, for its catalytic activity[1][3][5][10]. The enzyme is of significant interest as a potential antibacterial drug target due to its central role in regulating multicellular behaviors in pathogenic bacteria[3][5][7].

Other names

S-ribosylhomocysteinaseLuxSS-(5-deoxy-D-ribos-5-yl)-L-homocysteine L-homocysteine-lyase [(4S)-4,5-dihydroxypentan-2,3-dione-forming]

Inhibition of quorum sensing, Disruption of AI-2 signaling pathway, Interference with bacterial communication and virulence