LuxS is a
homodimeric iron-dependent
metalloenzyme containing two identical
tetrahedral metal-binding sites similar to those found in
peptidases and
amidases. Furthermore, LuxS is involved in the
synthesis of
autoinducer AI-2 (
autoinducer-2), which mediates
quorum sensing in roughly half of bacterial species. AI-2, a furanosyl borate diester, is a small
signaling molecule generated by bacteria. LuxS converts S-ribosylhomocysteine to
homocysteine and 4,5-dihydroxy-2,3-pentanedione (DPD); DPD can then spontaneously cyclisize to active AI-2. AI-2 is a
signalling molecule that is believed to act in cross-species communication by regulating niche-specific
genes with diverse functions, such as toxin production, biofilm formation, sporulation, and virulence gene expression, in various
bacteria, often in response to
population density. The AI-2 formation pathway begins with
S-adenosyl-L-homocysteine (AdoHcy), which is hydrolyzed to
S-adenosyl-L-homocysteine (SRH) and adenine by
S-adenosyl-L-homocysteine/5’-methylthioadenosine nucleosidase (SAHN or MTAN, EC 3.2.2.9) (8-10). LuxS cleaves S-ribosyl-homocysteine to form L-
homocysteine (Hcy) and 4,5-dihydroxy-2,3-pentanedione (DPD), which can then spontaneously cyclisize to active AI-2 (11-15). Thus, while it is certainly true that some bacteria can respond to AI-2, it is doubtful that it is always being produced for purposes of signaling. == Clinical significance ==