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Characterization of S-Ribosylhomocysteinase (LuxS)
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230 b
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S-Ribosylhomocysteinase (LuxS) catalyzes the cleavage§of the §thioether bond in S-ribosylhomocysteine to produce L-§homocysteine and 4,5-dihydroxy-2,3-pentanedione,§the precursor of type II bacterial quorum sensing§autoinducer. §This work carried out extensive mechanistic studies§of the LuxS §reaction. The native metal cofactor of LuxS was§identified as ferrous §ion, instead of previously reported zinc ion, with a§potential catalytic §role. Substantial evidence was provided for the§internal redox §reaction, which comprised two consecutive carbonyl§migration steps §followed by -elimination. §Three LuxS activity assays were developed and greatly§facilitated the §mechanistic investigations of LuxS. Two classes of§LuxS inhibitors §were designed based on metal chelation and catalytic§mechanism, §respectively. They encouraged future development of§LuxS inhibitors §as novel antibacterial agents and helped probe the§catalytic §mechanism of LuxS.
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