http://purl.uniprot.org/citations/9804843 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9804843 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9804843 | http://www.w3.org/2000/01/rdf-schema#comment | "Saccharomyces cerevisiae csg2Delta mutants accumulate the sphingolipid inositolphosphorylceramide, which renders the cells Ca2+-sensitive. Temperature-sensitive mutations that suppress the Ca2+ sensitivity of csg2Delta mutants were isolated and characterized to identify genes that encode sphingolipid synthesis enzymes. These temperature-sensitive csg2Delta suppressors (tsc) fall into 15 complementation groups. The TSC10/YBR265w gene was found to encode 3-ketosphinganine reductase, the enzyme that catalyzes the second step in the synthesis of phytosphingosine, the long chain base found in yeast sphingolipids. 3-Ketosphinganine reductase (Tsc10p) is essential for growth in the absence of exogenous dihydrosphingosine or phytosphingosine. Tsc10p is a member of the short chain dehydrogenase/reductase protein family. The tsc10 mutants accumulate 3-ketosphinganine and microsomal membranes isolated from tsc10 mutants have low 3-ketosphinganine reductase activity. His6-tagged Tsc10p was expressed in Escherichia coli and isolated by nickel-nitrilotriacetic acid column chromatography. The recombinant protein catalyzes the NADPH-dependent reduction of 3-ketosphinganine. These data indicate that Tsc10p is necessary and sufficient for catalyzing the NADPH-dependent reduction of 3-ketosphinganine to dihydrosphingosine."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.273.46.30688"xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.273.46.30688"xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Johnson C."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Johnson C."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Beeler T."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Beeler T."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Dunn T."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Dunn T."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Gable K."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Gable K."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Hopkins L."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Hopkins L."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Bacikova D."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Bacikova D."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Slife H."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/author | "Slife H."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/pages | "30688-30694"xsd:string |
http://purl.uniprot.org/citations/9804843 | http://purl.uniprot.org/core/pages | "30688-30694"xsd:string |