| http://purl.uniprot.org/citations/23263199 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23263199 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23263199 | http://www.w3.org/2000/01/rdf-schema#comment | "Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates. It contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153). The current study considers the functional role of these potential N-glycosylations within the enzyme. We produced truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain. To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system. After production and purification of these variants of human FucT IX, the wild-type (wt) enzyme and the variants were characterized regarding their activity and kinetic properties. The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters. While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity. The same could be observed for variants missing two or more putative N-glycosylation sites, which indicated the importance of N-glycosylation for enzyme stability and activity."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.org/dc/terms/identifier | "doi:10.1093/glycob/cws219"xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.org/dc/terms/identifier | "doi:10.1093/glycob/cws219"xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/author | "Hahn U."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/author | "Hahn U."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/author | "Seelhorst K."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/author | "Seelhorst K."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/author | "Stacke C."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/author | "Stacke C."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/author | "Ziegelmueller P."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/author | "Ziegelmueller P."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/name | "Glycobiology"xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/name | "Glycobiology"xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/pages | "559-567"xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/pages | "559-567"xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/title | "N-glycosylations of human alpha1,3-fucosyltransferase IX are required for full enzyme activity."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/title | "N-glycosylations of human alpha1,3-fucosyltransferase IX are required for full enzyme activity."xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/volume | "23"xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://purl.uniprot.org/core/volume | "23"xsd:string |
| http://purl.uniprot.org/citations/23263199 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23263199 |
| http://purl.uniprot.org/citations/23263199 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23263199 |