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http://purl.uniprot.org/citations/10913825http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10913825http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10913825http://www.w3.org/2000/01/rdf-schema#comment"We have identified two genomic DNA fragments from the human pathogenic fungi, Candida albicans (CaVIG9) and Candida glabrata (CgVIG9) that encode GDP-mannose pyrophosphorylase, a key enzyme for protein glycosylation. The VIG9 homologues of CaVIG9 and CgVIG9 complement an identified protein glycosylation-defective mutation, vig9, of Saccharomyces cerevisiae. The nucleotide sequences of the ORFs, which are 83 and 90% identical to that of the ScVIG9 protein, respectively, showed a predicted gene product homologous to S. cerevisiae GDP-mannose pyrophosphorylase. We examined the enzyme activity of a glutathione S-transferase fusion of each VIG9 gene to synthesize GDP mannose in the cell extracts of a heterologous Escherichia coli expression system. We also developed a method for detecting the enzyme activity using a non-radioactive substrate that would be applicable to high throughput screening."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.org/dc/terms/identifier"doi:10.1016/s0304-4165(00)00075-1"xsd:string
http://purl.uniprot.org/citations/10913825http://purl.org/dc/terms/identifier"doi:10.1016/s0304-4165(00)00075-1"xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/author"Chibana H."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/author"Chibana H."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/author"Ohta A."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/author"Ohta A."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/author"Arisawa M."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/author"Arisawa M."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/author"Sudoh M."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/author"Sudoh M."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/pages"265-272"xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/pages"265-272"xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/title"The VIG9 gene products from the human pathogenic fungi Candida albicans and Candida glabrata encode GDP-mannose pyrophosphorylase."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/title"The VIG9 gene products from the human pathogenic fungi Candida albicans and Candida glabrata encode GDP-mannose pyrophosphorylase."xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/volume"1475"xsd:string
http://purl.uniprot.org/citations/10913825http://purl.uniprot.org/core/volume"1475"xsd:string
http://purl.uniprot.org/citations/10913825http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10913825
http://purl.uniprot.org/citations/10913825http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10913825