| http://purl.uniprot.org/citations/12956060 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12956060 | http://www.w3.org/2000/01/rdf-schema#comment | "The stereochemical course of the dihydroceramide delta 4-(E)-desaturase from Candida albicans, cloned and expressed in the yeast Saccharomyces cerevisiae strain sur2 delta, was determined using stereospecifically labelled (2R,3S)-[2,3,4,4-2H4]-palmitic acid as a metabolic probe. Mass spectrometric analysis of the dinitrophenyl-derivatives of the labelled long-chain bases revealed elimination of a single deuterium atom from C(4) (corresponding to the C(4)-HR) along with a hydrogen atom from C(5) (corresponding to the C(5)-HS). This finding is consistent with an overall syn-elimination of the two vicinal hydrogen atoms. Besides the desaturation product sphingosine (93%) minor amounts of a 4-hydroxylated product (phytosphinganine, 7%) were identified that classify the Candida enzyme as a bifunctional desaturase/hydroxylase. Both processes, desaturation and hydroxylation proceed with loss of C(4)-HR from the chiral precursor. This finding is in agreement with a two-step process involving activation of the substrate by removal of the C(4)-HR to give a C-centred radical or radicaloid followed by either disproportionation into an olefin, water and a reduced diiron complex, or to recombination of the primary reactive intermediate with an active site-bound oxygen to yield a secondary alcohol. This result demonstrates the close mechanistic relationship between desaturation and hydroxylation as two different reaction pathways of a single enzyme and strengthens the mechanistic relationship of desaturases from fatty acid metabolism and sphingolipids."xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://purl.org/dc/terms/identifier | "doi:10.1039/b303939k"xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://purl.uniprot.org/core/author | "Heinz E."xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://purl.uniprot.org/core/author | "Sperling P."xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://purl.uniprot.org/core/author | "Boland W."xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://purl.uniprot.org/core/author | "Beckmann C."xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://purl.uniprot.org/core/author | "Rattke J."xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12956060 | http://purl.uniprot.org/core/name | "Org Biomol Chem"xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://purl.uniprot.org/core/pages | "2448-2454"xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://purl.uniprot.org/core/title | "Stereochemistry of a bifunctional dihydroceramide delta 4-desaturase/hydroxylase from Candida albicans; a key enzyme of sphingolipid metabolism."xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://purl.uniprot.org/core/volume | "1"xsd:string |
| http://purl.uniprot.org/citations/12956060 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12956060 |
| http://purl.uniprot.org/citations/12956060 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12956060 |
| http://purl.uniprot.org/uniprot/#_P38992-mappedCitation-12956060 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/12956060 |
| http://purl.uniprot.org/uniprot/P38992 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/12956060 |