Abstract:
:The production of toxins A and B by Clostridium difficile was greatly enhanced under biotin-limited conditions, in which a 140-kDa protein was expressed strongly. Gene cloning revealed that this protein was a homologue of formylglycinamidine ribonucleotide synthetase (FGAM synthetase, EC 6.3.5.3), which is known as PurL in Escherichia coli and catalyses the fourth step of the de novo purine biosynthesis pathway. This enzyme consisted of a single polypeptide, although FGAM synthetases of gram-positive bacteria usually consist of two subunits. Inhibition of the enzymic activity of C. difficile PurL by O-diazoacetyl-L-serine (azaserine) resulted in enhanced toxin B production even in biotin-sufficient conditions. In contrast, blockade of the preceding step of the PurL catalysing step by sulfamethoxazole inhibited toxin B production almost completely. These results suggest that accumulation of formylglycinamide ribonucleotide (FGAR), a substrate of FGAM synthetase, enhances toxin production by C difficile and depletion of FGAR reduces toxin production.
journal_name
J Med Microbioljournal_title
Journal of medical microbiologyauthors
Maegawa T,Karasawa T,Ohta T,Wang X,Kato H,Hayashi H,Nakamura Sdoi
10.1099/0022-1317-51-1-34keywords:
subject
Has Abstractpub_date
2002-01-01 00:00:00pages
34-41issue
1eissn
0022-2615issn
1473-5644journal_volume
51pub_type
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