http://purl.uniprot.org/citations/15632306 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15632306 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15632306 | http://www.w3.org/2000/01/rdf-schema#comment | "N-Acetylglucosamine 6-O-sulfotransferases (GlcNAc6STs) catalyze the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 position of non-reducing N-acetylglucosamine. N-acetylglucosamine 6-O-sulfotransferase-1 (GlcNAc6ST-1) is the first cloned GlcNAc6ST and is involved in the synthesis of the L-selectin ligand. We noticed conserved C-terminal segments among GlcNAc6STs and produced mutant enzymes to reveal the functional significance. Mutant enzymes were transiently expressed as fusion proteins with protein A in COS-7 cells, and some of them were purified to homogeneity by IgG Sepharose column chromatography. Deletion of a C-terminal segment (amino acid numbers 479-483) resulted in a complete loss of the activity, when assayed using GlcNAcbeta1-6ManOMe as a substrate. Upon site-directed mutagenesis of the C-terminal region, three mutants, L477A, L478A and L483A, exhibited reduced activity. The K(M )values for GlcNAcbeta1-6ManOMe of L477A and L478A were 4 times higher than the K(M) of the wild-type enzyme, while that of L483A was unchanged. On the other hand the K(M )for PAPS of L483A was 3 times higher than that of the wild-type enzyme, while the values of L477A and L478A were unchanged. Furthermore, the L477A mutant acted on a core 3 structure (GlcNAcbeta1-3GalNAc-pNP), while the wild-type enzyme does not. These results demonstrate a role for leucine residues in the C-terminal region in the enzymatic activity."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvh162"xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvh162"xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/author | "Chen L."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/author | "Chen L."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/author | "Muramatsu T."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/author | "Muramatsu T."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/author | "Ichihara-Tanaka K."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/author | "Ichihara-Tanaka K."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/pages | "659-664"xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/pages | "659-664"xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/title | "Role of the carboxyl-terminal region in the activity of N-acetylglucosamine 6-o-sulfotransferase-1."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/title | "Role of the carboxyl-terminal region in the activity of N-acetylglucosamine 6-o-sulfotransferase-1."xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/volume | "136"xsd:string |
http://purl.uniprot.org/citations/15632306 | http://purl.uniprot.org/core/volume | "136"xsd:string |
http://purl.uniprot.org/citations/15632306 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15632306 |
http://purl.uniprot.org/citations/15632306 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15632306 |
http://purl.uniprot.org/citations/15632306 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15632306 |
http://purl.uniprot.org/citations/15632306 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15632306 |