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http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/6.-.-.-
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/6.3.2.-
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/6.3.-.-
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2000/01/rdf-schema#comment"The enzymes from different sources (particularly eukaryotes versus prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates."xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2000/01/rdf-schema#comment"In contrast, the activities are located on separate proteins in most eukaryotes studied to date."xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2000/01/rdf-schema#comment"As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred cofactors of C1 metabolism."xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2000/01/rdf-schema#comment"Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes."xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2000/01/rdf-schema#comment"In Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast."xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2000/01/rdf-schema#comment"In some bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.12, the combined activity of which leads to the formation of the cofactor polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates (H4folate)."xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2004/02/skos/core#prefLabel"tetrahydrofolate synthase"xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10799479
http://purl.uniprot.org/enzyme/6.3.2.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11752472
http://purl.uniprot.org/enzyme/6.3.2.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/2985605
http://purl.uniprot.org/enzyme/6.3.2.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6458762
http://purl.uniprot.org/enzyme/6.3.2.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7027025
http://purl.uniprot.org/enzyme/6.3.2.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9190084
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2004/02/skos/core#altLabel"FPGS"xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2004/02/skos/core#altLabel"folylpolyglutamate synthase"xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2004/02/skos/core#altLabel"tetrahydrofolylpolyglutamate synthase"xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2004/02/skos/core#altLabel"folylpolyglutamate synthetase"xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2004/02/skos/core#altLabel"folate polyglutamate synthetase"xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2004/02/skos/core#altLabel"folylpoly(gamma-glutamate) synthase"xsd:string
http://purl.uniprot.org/enzyme/6.3.2.17http://www.w3.org/2004/02/skos/core#altLabel"folylpoly-gamma-glutamate synthase"xsd:string