<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Mattes TA</submitter><funding>National Institutes of Natural Sciences</funding><funding>U.S. Public Health Service</funding><funding>NIGMS NIH HHS</funding><pagination>269-281</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5218876</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>103(2)</volume><pubmed_abstract>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. </pubmed_abstract><journal>Molecular microbiology</journal><pubmed_title>Salmonella enterica synthesizes 5,6-dimethylbenzimidazolyl-(DMB)-α-riboside. Why some Firmicutes do not require the canonical DMB activation system to synthesize adenosylcobalamin.</pubmed_title><pmcid>PMC5218876</pmcid><funding_grant_id>R37 GM040313</funding_grant_id><funding_grant_id>R37 GM40313</funding_grant_id><pubmed_authors>Escalante-Semerena JC</pubmed_authors><pubmed_authors>Mattes TA</pubmed_authors></additional><is_claimable>false</is_claimable><name>Salmonella enterica synthesizes 5,6-dimethylbenzimidazolyl-(DMB)-α-riboside. Why some Firmicutes do not require the canonical DMB activation system to synthesize adenosylcobalamin.</name><description>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. </description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Jan</publication><modification>2025-04-04T01:31:33.95Z</modification><creation>2019-03-27T02:33:32Z</creation></dates><accession>S-EPMC5218876</accession><cross_references><pubmed>27748967</pubmed><doi>10.1111/mmi.13555</doi></cross_references></HashMap>