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http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.1.1.-
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.1.-.-
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2000/01/rdf-schema#comment"The enzymes from yeast and rat also catalyze the methylation of 3-demethylubiquinol-6 and 3-demethylubiquinol-9, respectively (this activity is classified as EC 2.1.1.64)."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2000/01/rdf-schema#comment"However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2000/01/rdf-schema#comment"Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2000/01/rdf-schema#comment"This enzyme is involved in ubiquinone biosynthesis."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2000/01/rdf-schema#comment"For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2004/02/skos/core#prefLabel"polyprenyldihydroxybenzoate methyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10419476
http://purl.uniprot.org/enzyme/2.1.1.114http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1885593
http://purl.uniprot.org/enzyme/2.1.1.114http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10777520
http://purl.uniprot.org/enzyme/2.1.1.114http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/21636923
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2004/02/skos/core#altLabel"3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2004/02/skos/core#altLabel"DHHB methyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2004/02/skos/core#altLabel"DHHB O-methyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2004/02/skos/core#altLabel"DHHB-Mt"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://www.w3.org/2004/02/skos/core#altLabel"dihydroxyhexaprenylbenzoate methyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.114http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.1.1.114#SIPC8755018E5D3D5B5
http://purl.uniprot.org/enzyme/2.1.1.114http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.1.1.114#SIP5A0BEE7CE4BEC209
http://purl.uniprot.org/enzyme/2.1.1.114http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.1.1.114#SIP645F1929795D6649
http://purl.uniprot.org/enzyme/2.1.1.114http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.1.1.114#SIPBA5B1EEF444EAAAB
http://purl.uniprot.org/enzyme/2.1.1.114http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.1.1.114#SIPC99F32E87B758CBB