Welkom bij het Lymeforum

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B. burgdorferi cannot utilize the other product of LuxS, homocysteine,
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Bacteria use S-adenosylmethionine (SAM) as the methyl donor for methylation reactions (Fig. 1). In many species, including B. burgdorferi, the resulting by-product, S-adenosylhomocysteine (SAH), is detoxified by Pfs to S-ribosylhomocysteine (SRH). That product, in turn, is broken down by LuxS into homocysteine and 4,5-dihydroxy-2,3-pentanedione (DPD) (4–9). Although some bacterial species are able to recycle homocysteine into methionine, genetic and biochemical analyses demonstrated that B. burgdorferi lacks the necessary enzymes and thus cannot use homocysteine (8, 10). Several bacterial species, including the syphilis spirochete, Treponema pallidum, produce a Pfs enzyme but lack LuxS, indicating that SRH is not inhibitory to bacterial growth (8, 11). These observations beg the question of why B. burgdorferi possesses a LuxS enzyme.
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