{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T02:01:32Z","timestamp":1768528892834,"version":"3.49.0"},"reference-count":27,"publisher":"American Society for Microbiology","issue":"16","license":[{"start":{"date-parts":[[2016,8,15]],"date-time":"2016-08-15T00:00:00Z","timestamp":1471219200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SCHU2605\/1-1"],"award-info":[{"award-number":["SCHU2605\/1-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001654","name":"DAAD | German Academic Exchange Service London","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001654","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["R37 GM040313"],"award-info":[{"award-number":["R37 GM040313"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2016,8,15]]},"abstract":"ABSTRACT<\/jats:title>\n \n The tetrachloroethene (PCE)-respiring bacterium\n Sulfurospirillum multivorans<\/jats:named-content>\n produces a unique cobamide, namely, norpseudo-B\n 12<\/jats:sub>\n , which, in comparison to other cobamides, e.g., cobalamin and pseudo-B\n 12<\/jats:sub>\n , lacks the methyl group in the linker moiety of the nucleotide loop. In this study, the protein SMUL_1544 was shown to be responsible for the formation of the unusual linker moiety, which is most probably derived from ethanolamine-phosphate (EA-P) as the precursor. The product of the\n SMUL_1544<\/jats:italic>\n gene successfully complemented a\n Salmonella enterica<\/jats:named-content>\n \u0394\n cobD<\/jats:italic>\n mutant. The\n cobD<\/jats:italic>\n gene encodes an\n l<\/jats:sc>\n -threonine-\n O<\/jats:italic>\n -3-phosphate (\n l<\/jats:sc>\n -Thr-P) decarboxylase responsible for the synthesis of (\n R<\/jats:italic>\n )-1-aminopropan-2-ol\n O<\/jats:italic>\n -2-phosphate (AP-P), required specifically for cobamide biosynthesis. When SMUL_1544 was produced in the heterologous host lacking CobD, norpseudo-B\n 12<\/jats:sub>\n was formed, which pointed toward the formation of EA-P rather than AP-P. Guided cobamide biosynthesis experiments with minimal medium supplemented with\n l<\/jats:sc>\n -Thr-P supported cobamide biosynthesis in\n S. enterica<\/jats:named-content>\n producing SMUL_1544 or\n S. multivorans<\/jats:named-content>\n . Under these conditions, both microorganisms synthesized pseudo-B\n 12<\/jats:sub>\n . This observation indicated a flexibility in the SMUL_1544 substrate spectrum. From the formation of catalytically active PCE reductive dehalogenase (PceA) in\n S. multivorans<\/jats:named-content>\n cells producing pseudo-B\n 12<\/jats:sub>\n , a compatibility of the respiratory enzyme with the cofactor was deduced. This result might indicate a structural flexibility of PceA in cobamide binding. Feeding of\n l<\/jats:sc>\n -[3-\n 13<\/jats:sup>\n C]serine to cultures of\n S. multivorans<\/jats:named-content>\n resulted in isotope labeling of the norpseudo-B\n 12<\/jats:sub>\n linker moiety, which strongly supports the hypothesis of EA-P formation from\n l<\/jats:sc>\n -serine-\n O<\/jats:italic>\n -phosphate (\n l<\/jats:sc>\n -Ser-P) in this organism.\n <\/jats:p>\n \n IMPORTANCE<\/jats:bold>\n The identification of the gene product SMUL_1544 as a putative\n l<\/jats:sc>\n -Ser-P decarboxylase involved in norcobamide biosynthesis in\n S. multivorans<\/jats:named-content>\n adds a novel module to the assembly line of cobamides (complete corrinoids) in prokaryotes. Selected cobamide-containing enzymes (e.g., reductive dehalogenases) showed specificity for their cobamide cofactors. It has recently been proposed that the structure of the linker moiety of norpseudo-B\n 12<\/jats:sub>\n and the mode of binding of the EA-P linker to the PceA enzyme reflect the high specificity of the enzyme for its cofactor. Data reported herein do not support this idea. In fact, norpseudo-B\n 12<\/jats:sub>\n was functional in the cobamide-dependent methionine biosynthesis of\n S. enterica<\/jats:named-content>\n , raising questions about the role of norcobamides in nature.\n <\/jats:p>","DOI":"10.1128\/jb.00289-16","type":"journal-article","created":{"date-parts":[[2016,6,7]],"date-time":"2016-06-07T03:14:04Z","timestamp":1465269244000},"page":"2236-2243","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":20,"title":["The\n SMUL_1544<\/i>\n Gene Product Governs Norcobamide Biosynthesis in the Tetrachloroethene-Respiring Bacterium Sulfurospirillum multivorans"],"prefix":"10.1128","volume":"198","author":[{"given":"Sebastian","family":"Keller","sequence":"first","affiliation":[{"name":"Department of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, Jena, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aaron","family":"Treder","sequence":"additional","affiliation":[{"name":"Department of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, Jena, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephan H.","family":"von Reuss","sequence":"additional","affiliation":[{"name":"Department of Bioorganic Chemistry, Max Planck Institute for Chemical Ecology, Jena, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jorge C.","family":"Escalante-Semerena","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Georgia, Athens, Georgia, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Torsten","family":"Schubert","sequence":"additional","affiliation":[{"name":"Department of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, Jena, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1039\/b108967f"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.72.121801.161828"},{"key":"e_1_3_2_4_2","first-page":"1","volume-title":"Wiley encyclopedia of chemical biology","author":"Buckel W","year":"2008","unstructured":"Buckel W, Golding BT. 2008. 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