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• W2533262007 abstract "Summary 5,6‐Dimethylbenzimidazolyl‐(DMB)‐ α ‐ribotide [ α ‐ribazole‐5′‐phosphate ( α ‐RP)] is an intermediate in the biosynthesis of adenosylcobalamin (AdoCbl) in many prokaryotes. In such microbes, α ‐RP is synthesized by nicotinate mononucleotide (NaMN):DMB phosphoribosyltransferases (CobT in Salmonella enterica ), in a reaction that is considered to be the canonical step for the activation of the base of the nucleotide present in adenosylcobamides. Some Firmicutes lack CobT‐type enzymes but have a two‐protein system comprised of a transporter ( i.e ., CblT) and a kinase ( i.e. , CblS) that can salvage exogenous α ‐ribazole ( α ‐R) from the environment using CblT to take up α ‐R, followed by α ‐R phosphorylation by CblS. We report that Geobacillus kaustophilus CblT and CblS proteins restore α ‐RP synthesis in S. enterica lacking the CobT enzyme. We also show that a S. enterica cobT strain that synthesizes Gk CblS ectopically makes only AdoCbl, even under growth conditions where the synthesis of pseudoCbl is favored. Our results indicate that S. enterica synthesizes α ‐R, a metabolite that had not been detected in this bacterium and that Gk CblS has a strong preference for DMB‐ribose over adenine‐ribose as substrate. We propose that in some Firmicutes DMB is activated to α ‐RP via α ‐R using an as‐yet‐unknown route to convert DMB to α ‐R and CblS to convert α ‐R to α ‐RP." @default.
• W2533262007 created "2016-10-28" @default.
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• W2533262007 date "2016-11-22" @default.
• W2533262007 modified "2023-10-04" @default.
• W2533262007 title "<i>Salmonella enterica</i>synthesizes 5,6-dimethylbenzimidazolyl-(DMB)-α-riboside. Why some Firmicutes do not require the canonical DMB activation system to synthesize adenosylcobalamin" @default.
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• W2533262007 doi "https://doi.org/10.1111/mmi.13555" @default.
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