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In this work we investigated the enzymes involved in the biosynthesis of thymidine diphospho-\n            <jats:sc>l<\/jats:sc>\n            -rhamnose (dTDP-\n            <jats:sc>l<\/jats:sc>\n            -rhamnose) and their specific properties. Comparable to lipopolysaccharide O-antigen biosynthesis in gram-negative bacteria, dTDP-\n            <jats:sc>l<\/jats:sc>\n            -rhamnose is synthesized in a four-step reaction sequence from dTTP and glucose 1-phosphate by the enzymes glucose-1-phosphate thymidylyltransferase (RmlA), dTDP-\n            <jats:sc>d<\/jats:sc>\n            -glucose 4,6-dehydratase (RmlB), dTDP-4-dehydrorhamnose 3,5-epimerase (RmlC), and dTDP-4-dehydrorhamnose reductase (RmlD). The rhamnose biosynthesis operon from\n            <jats:italic>A. thermoaerophilus<\/jats:italic>\n            DSM 10155 was sequenced, and the genes were overexpressed in\n            <jats:italic>Escherichia coli<\/jats:italic>\n            . Compared to purified enterobacterial Rml enzymes, the enzymes from the gram-positive strain show remarkably increased thermostability, a property which is particularly interesting for high-throughput screening and enzymatic synthesis. The closely related strain\n            <jats:italic>A. thermoaerophilus<\/jats:italic>\n            L420-91\n            <jats:sup>T<\/jats:sup>\n            produces\n            <jats:sc>d<\/jats:sc>\n            -rhamnose- and 3-acetamido-3,6-dideoxy-\n            <jats:sc>d<\/jats:sc>\n            -galactose-containing S-layer glycan chains. Comparison of the enzyme activity patterns in\n            <jats:italic>A. thermoaerophilus<\/jats:italic>\n            strains DSM 10155 and L420-91\n            <jats:sup>T<\/jats:sup>\n            for\n            <jats:sc>l<\/jats:sc>\n            -rhamnose and\n            <jats:sc>d<\/jats:sc>\n            -rhamnose biosynthesis indicated that the enzymes are differentially expressed during S-layer glycan biosynthesis and that\n            <jats:italic>A. thermoaerophilus<\/jats:italic>\n            L420-91\n            <jats:sup>T<\/jats:sup>\n            is not able to synthesize dTDP-\n            <jats:sc>l<\/jats:sc>\n            -rhamnose. These findings confirm that in each strain the enzymes act specifically on S-layer glycoprotein glycan formation.\n          <\/jats:p>","DOI":"10.1128\/aem.68.8.3708-3715.2002","type":"journal-article","created":{"date-parts":[[2002,10,1]],"date-time":"2002-10-01T19:36:19Z","timestamp":1033500979000},"page":"3708-3715","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":44,"title":["Homologs of the Rml Enzymes from\n            <i>Salmonella enterica<\/i>\n            Are Responsible for dTDP-\u03b2-\n            <scp>l<\/scp>\n            -Rhamnose Biosynthesis in the Gram-Positive Thermophile\n            <i>Aneurinibacillus thermoaerophilus<\/i>\n            DSM 10155"],"prefix":"10.1128","volume":"68","author":[{"given":"Michael","family":"Graninger","sequence":"first","affiliation":[{"name":"Zentrum fu\u0308r Ultrastrukturforschung und Ludwig Boltzmann-Institut fu\u0308r Molekulare Nanotechnologie, Universita\u0308t fu\u0308r Bodenkultur Wien, A-1180 Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bernd","family":"Kneidinger","sequence":"additional","affiliation":[{"name":"Zentrum fu\u0308r Ultrastrukturforschung und Ludwig Boltzmann-Institut fu\u0308r Molekulare Nanotechnologie, Universita\u0308t fu\u0308r Bodenkultur Wien, A-1180 Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katharina","family":"Bruno","sequence":"additional","affiliation":[{"name":"Zentrum fu\u0308r Ultrastrukturforschung und Ludwig Boltzmann-Institut fu\u0308r Molekulare Nanotechnologie, Universita\u0308t fu\u0308r Bodenkultur Wien, A-1180 Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Scheberl","sequence":"additional","affiliation":[{"name":"Zentrum fu\u0308r Ultrastrukturforschung und Ludwig Boltzmann-Institut fu\u0308r Molekulare Nanotechnologie, Universita\u0308t fu\u0308r Bodenkultur Wien, A-1180 Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul","family":"Messner","sequence":"additional","affiliation":[{"name":"Zentrum fu\u0308r Ultrastrukturforschung und Ludwig Boltzmann-Institut fu\u0308r Molekulare Nanotechnologie, Universita\u0308t fu\u0308r Bodenkultur Wien, A-1180 Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/25.17.3389"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1996.711442.x"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.171.8.4178-4188.1989"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/16.22.10881"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1996.tb02469.x"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0959-440X(00)00145-7"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)63305-3"},{"key":"e_1_3_2_10_2","first-page":"1","volume":"3","year":"1974","unstructured":"Glauert, A. 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