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http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.5.1.-
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.5.-.-
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2000/01/rdf-schema#comment"The reaction occurs in four steps: NAD(+)-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d)."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2000/01/rdf-schema#comment"For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2000/01/rdf-schema#comment"Hence the overall reaction is transfer of a 4-aminobutyl group."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2000/01/rdf-schema#comment"The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2000/01/rdf-schema#comment"Catalyzes the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2000/01/rdf-schema#comment"Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2004/02/skos/core#prefLabel"deoxyhypusine synthase"xsd:string
http://purl.uniprot.org/enzyme/2.5.1.46http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10542236
http://purl.uniprot.org/enzyme/2.5.1.46http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10611289
http://purl.uniprot.org/enzyme/2.5.1.46http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7592594
http://purl.uniprot.org/enzyme/2.5.1.46http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7673224
http://purl.uniprot.org/enzyme/2.5.1.46http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10028184
http://purl.uniprot.org/enzyme/2.5.1.46http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10734052
http://purl.uniprot.org/enzyme/2.5.1.46http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/2108161
http://purl.uniprot.org/enzyme/2.5.1.46http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9188485
http://purl.uniprot.org/enzyme/2.5.1.46http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9285092
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2004/02/skos/core#altLabel"spermidine dehydrogenase"xsd:string
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2004/02/skos/core#altLabel"(4-aminobutyl)lysine synthase"xsd:string
http://purl.uniprot.org/enzyme/2.5.1.46http://www.w3.org/2004/02/skos/core#altLabel"[eIF-5A]-deoxyhypusine synthase"xsd:string
http://purl.uniprot.org/enzyme/2.5.1.46http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/1.1.1.249