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        <identifier>oai:www.ideals.illinois.edu:2142/84881</identifier>
        <datestamp>2023-07-11</datestamp>
        <setSpec>col_2142_5131</setSpec>
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        <thesis xmlns="http://www.ndltd.org/standards/metadata/etdms/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:dc="http://purl.org/dc/elements/1.1/" xsi:schemaLocation="http://www.ndltd.org/standards/metadata/etdms/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdms11.xsd http://purl.org/dc/elements/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdmsdc.xsd">
          <dc:contributor>Peter A.B.Orlean</dc:contributor>
          <dc:creator>Colussi, Paul Attilio</dc:creator>
          <dc:date>2015-09-25T22:28:19Z</dc:date>
          <dc:date>2015-09-25T22:28:19Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>1997</dc:date>
          <dc:date>1997</dc:date>
          <dc:description>I cloned cDNAs encoding S. pombe, human and Caenorhabditis briggsiae Dol-P-Man synthases, all three of which lack a characteristic carboxy-terminal transmembrane region found on previously isolated Dol-P-Man synthases. Known Dol-P-Man synthases can therefore be divided into a 'human' or 'S. cerevisiae' class, although the two are functionally equivalent for I showed that the S. cerevisiae DPM1 gene and its human counterpart both complement the lethal dpm1$\sp+$ null mutation in S. pombe. The 'human' class of Dol-P-Man synthases, however, do not complement an S. cerevisiae dpm1 null mutant, and, unlike the S. cerevisiae class of enzymes, do not confer Dol-P-Man synthetic activity on E. coli cells. I propose that the 'human' class of Dol-P-Man synthase requires one or more auxiliary proteins for catalytic activity or to mediate membrane association. The facts that Dol-P-Man synthase is an essential enzyme in yeast, and that the Ustilago and Trypanosoma synthases are in a different class from the human enzyme, raises the possibility that Dol-P-Man synthase could be exploited as a target for selective inhibitors of pathogenic eukaryotic microbes.</dc:description>
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license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5)
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  Previous issue date: 1997</dc:description>
          <dc:description>Embargo set by: Seth Robbins for item 86162
Lift date: Forever
Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:description>147 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1997.</dc:description>
          <dc:identifier>http://hdl.handle.net/2142/84881</dc:identifier>
          <dc:identifier>(MiAaPQ)AAI9737080</dc:identifier>
          <dc:language>eng</dc:language>
          <dc:subject>Biology, Microbiology</dc:subject>
          <dc:title>Essential Glycosyltransferases in Schizosaccharomyces Pombe</dc:title>
          <dc:type>text</dc:type>
          <degree>
            <department>Biochemistry</department>
            <discipline>Biochemistry</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
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