http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/6.-.-.- |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/6.3.2.- |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/6.3.-.- |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://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/6.3.2.17 | http://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/6.3.2.17 | http://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/6.3.2.17 | http://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/6.3.2.17 | http://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/6.3.2.17 | http://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/6.3.2.17 | http://www.w3.org/2004/02/skos/core#prefLabel | "tetrahydrofolate synthase"xsd:string |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10799479 |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11752472 |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2985605 |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/6458762 |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7027025 |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9190084 |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2004/02/skos/core#altLabel | "FPGS"xsd:string |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2004/02/skos/core#altLabel | "folylpolyglutamate synthase"xsd:string |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2004/02/skos/core#altLabel | "tetrahydrofolylpolyglutamate synthase"xsd:string |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2004/02/skos/core#altLabel | "folylpolyglutamate synthetase"xsd:string |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2004/02/skos/core#altLabel | "folate polyglutamate synthetase"xsd:string |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2004/02/skos/core#altLabel | "folylpoly(gamma-glutamate) synthase"xsd:string |
http://purl.uniprot.org/enzyme/6.3.2.17 | http://www.w3.org/2004/02/skos/core#altLabel | "folylpoly-gamma-glutamate synthase"xsd:string |