http://purl.uniprot.org/citations/15616122 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15616122 | http://www.w3.org/2000/01/rdf-schema#comment | "Mucin-type O-glycosylation in Dictyostelium is initiated in the Golgi by a UDP-GlcNAc:polypeptide-Thr/Ser N-acetyl-alpha-glucosaminyltransferase (Dd-pp alphaGlcNAcT2) whose sequence is distantly related to the sequences of animal polypeptide-Thr/Ser N-acetyl-alpha-galactosaminyltransferases, such as murine Mm-pp alphaGalNAcT1. To evaluate the significance of this similarity, highly purified Dd-pp alphaGlcNAcT2 was assayed using synthetic peptides derived from known substrates. Dd-pp alphaGlcNAcT2 strongly prefers UDP-GlcNAc over UDP-GalNAc, preferentially modifies the central region of the peptide, and modifies Ser in addition to Thr residues. Initial velocity measurements performed over a matrix of UDP-GlcNAc donor and peptide acceptor concentrations indicate that the substrates bind to the enzyme in ordered fashion before the chemical conversion. Substrate inhibition exerted by a second peptide, and the pattern of product inhibition exerted by UDP, suggest that UDP-GlcNAc binds first and the peptide binds second, consistent with data reported for Mm-pp alphaGalNAcT1. Two selective competitive inhibitors of Mm-pp alphaGalNAcT1, retrieved from a screen of neutral-charge uridine derivatives, also inhibit Dd-pp alphaGlcNAcT1 competitively with only slightly less efficacy. Inhibition is specific for Dd-pp alphaGlcNAcT2 relative to two other Dictyostelium retaining glycosyltransferases. These data support a phylogenetic model in which the alphaGlcNAcT function in unicellular eukaryotes converted to an alphaGalNAcT function in the metazoan ortholog while conserving a similar reaction mechanism and active site architecture."xsd:string |
http://purl.uniprot.org/citations/15616122 | http://purl.org/dc/terms/identifier | "doi:10.1093/glycob/cwi034"xsd:string |
http://purl.uniprot.org/citations/15616122 | http://purl.uniprot.org/core/author | "Ercan A."xsd:string |
http://purl.uniprot.org/citations/15616122 | http://purl.uniprot.org/core/author | "West C.M."xsd:string |
http://purl.uniprot.org/citations/15616122 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15616122 | http://purl.uniprot.org/core/name | "Glycobiology"xsd:string |
http://purl.uniprot.org/citations/15616122 | http://purl.uniprot.org/core/pages | "489-500"xsd:string |
http://purl.uniprot.org/citations/15616122 | http://purl.uniprot.org/core/title | "Kinetic analysis of a Golgi UDP-GlcNAc:polypeptide-Thr/Ser N-acetyl-alpha-glucosaminyltransferase from Dictyostelium."xsd:string |
http://purl.uniprot.org/citations/15616122 | http://purl.uniprot.org/core/volume | "15"xsd:string |
http://purl.uniprot.org/citations/15616122 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15616122 |
http://purl.uniprot.org/citations/15616122 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15616122 |
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http://purl.uniprot.org/uniprot/Q8T1C6 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15616122 |
http://purl.uniprot.org/uniprot/Q54EX6 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15616122 |
http://purl.uniprot.org/uniprot/Q54RP0 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15616122 |