Absent in human, the LuxS enzyme (S-ribosylhomocysteinase) is an attractive target for novel therapeutic agent development for bacterial infection.  The enzyme LuxS cleaves S-ribosylhomocysteine (SRH) to form L-homocysteine and 4,5-dihydroxy-2,3-pentanedione which spontaneously cyclizes and complexes with borate to form furanosyl borate diester as autoinducers.  We have synthesized the 3-deoxy analogues of SRH 1 as potential inhibitors and mechanistic probes for LuxS since 3-deoxy analogues can not participate in the second enolization step to generate 3-keto derivatives because of the lack of 3-hydroxyl group. Thus, treatment of the 5-O-mesylate 2, derived from 3-deoxyribose, with homocysteine in the presence of aqueous sodium hydroxide followed by removal of isopropylidene protection group afforded 3-deoxy-SRH analogue 1 (a/β, 1:3).