{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,31]],"date-time":"2025-10-31T07:15:55Z","timestamp":1761894955205},"reference-count":34,"publisher":"American Society for Microbiology","issue":"19","license":[{"start":{"date-parts":[[2009,10,1]],"date-time":"2009-10-01T00:00:00Z","timestamp":1254355200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2009,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            In addition to di-\n            <jats:italic>myo<\/jats:italic>\n            -inositol-1,3\u2032-phosphate (DIP), a compatible solute widespread in hyperthermophiles, the organic solute pool of\n            <jats:italic>Thermotoga maritima<\/jats:italic>\n            comprises 2-(\n            <jats:italic>O<\/jats:italic>\n            -\u03b2-\n            <jats:sc>d-<\/jats:sc>\n            mannosyl)-di-\n            <jats:italic>myo<\/jats:italic>\n            -inositol-1,3\u2032-phosphate (MDIP) and 2-(\n            <jats:italic>O<\/jats:italic>\n            -\u03b2-\n            <jats:sc>d-<\/jats:sc>\n            mannosyl-1,2-\n            <jats:italic>O<\/jats:italic>\n            -\u03b2-\n            <jats:sc>d-<\/jats:sc>\n            mannosyl)-di-\n            <jats:italic>myo<\/jats:italic>\n            -inositol-1,3\u2032-phosphate (MMDIP), two newly identified \u03b2-1,2-mannosides. In cells grown under heat stress, MDIP was the major solute, accounting for 43% of the total pool; MMDIP and DIP accumulated to similar levels, each corresponding to 11.5% of the total pool. The synthesis of MDIP involved the transfer of the mannosyl group from GDP-mannose to DIP in a single-step reaction catalyzed by MDIP synthase. This enzyme used MDIP as an acceptor of a second mannose residue, yielding the di-mannosylated compound. Minor amounts of the tri-mannosylated form were also detected. With a genomic approach, putative genes for MDIP synthase were identified in the genome of\n            <jats:italic>T. maritima<\/jats:italic>\n            , and the assignment was confirmed by functional expression in\n            <jats:italic>Escherichia coli<\/jats:italic>\n            . Genes with significant sequence identity were found only in the genomes of\n            <jats:italic>Thermotoga<\/jats:italic>\n            spp.,\n            <jats:italic>Aquifex aeolicus<\/jats:italic>\n            , and\n            <jats:italic>Archaeoglobus profundus<\/jats:italic>\n            . MDIP synthase of\n            <jats:italic>T. maritima<\/jats:italic>\n            had maximal activity at 95\u00b0C and apparent\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            values of 16 mM and 0.7 mM for DIP and GDP-mannose, respectively. The stereochemistry of MDIP was characterized by isotopic labeling and nuclear magnetic resonance (NMR): DIP selectively labeled with carbon 13 at position C1 of the\n            <jats:sc>l-<\/jats:sc>\n            inositol moiety was synthesized and used as a substrate for MDIP synthase. This \u03b2-1,2-mannosyltransferase is unrelated to known glycosyltransferases, and within the domain\n            <jats:italic>Bacteria<\/jats:italic>\n            , it is restricted to members of the two deepest lineages, i.e., the\n            <jats:italic>Thermotogales<\/jats:italic>\n            and the\n            <jats:italic>Aquificales<\/jats:italic>\n            . To our knowledge, this is the first \u03b2-1,2-mannosyltransferase characterized thus far.\n          <\/jats:p>","DOI":"10.1128\/jb.00598-09","type":"journal-article","created":{"date-parts":[[2009,8,1]],"date-time":"2009-08-01T01:10:02Z","timestamp":1249089002000},"page":"6105-6115","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":17,"title":["A Unique \u03b2-1,2-Mannosyltransferase of\n            <i>Thermotoga maritima<\/i>\n            That Uses Di-\n            <i>myo<\/i>\n            -Inositol Phosphate as the Mannosyl Acceptor"],"prefix":"10.1128","volume":"191","author":[{"given":"Marta V.","family":"Rodrigues","sequence":"first","affiliation":[{"name":"Instituto de Tecnologia Qui\u0301mica e Biolo\u0301gica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156 Oeiras, Portugal"}]},{"given":"Nuno","family":"Borges","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qui\u0301mica e Biolo\u0301gica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156 Oeiras, Portugal"}]},{"given":"Carla P.","family":"Almeida","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qui\u0301mica e Biolo\u0301gica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156 Oeiras, Portugal"}]},{"given":"Pedro","family":"Lamosa","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qui\u0301mica e Biolo\u0301gica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156 Oeiras, Portugal"}]},{"given":"Helena","family":"Santos","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qui\u0301mica e Biolo\u0301gica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156 Oeiras, Portugal"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj2580001","volume":"258","year":"1989","unstructured":"Anonymous. 1989. 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