| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.8.1.- |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.8.-.- |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein."xsd:string |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "Having donated two sulfur atoms, the auxiliary cluster is degraded during catalysis, but is regenerated immediately by the transfer of a new cluster from iron-sulfur cluster carrier proteins."xsd:string |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "An alternative lipoylation pathway involves EC 6.3.1.20, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs)."xsd:string |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "It is a member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (S-adenosylmethionine) by the addition of an electron from an iron-sulfur center."xsd:string |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme contains two [4Fe-4S] clusters."xsd:string |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "The first cluster produces the radicals, which are converted into 5'-deoxyadenosine when they abstract hydrogen atoms from C6 and C8, respectively, leaving reactive radicals at these positions that interact with sulfur atoms within the second (auxiliary) cluster."xsd:string |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "This enzyme catalyzes the final step in the de novo biosynthesis of the lipoyl cofactor, the attachment of two sulfhydryl groups to C6 and C8 of a pendant octanoyl chain."xsd:string |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein)."xsd:string |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2004/02/skos/core#prefLabel | "lipoyl synthase"xsd:string |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1655709 |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9218413 |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11106496 |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/14700636 |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15157071 |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15740115 |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/29051382 |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10966480 |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2004/02/skos/core#altLabel | "lipoate synthase"xsd:string |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/2.8.1.8#SIPB6F379EC8586E313 |
| http://purl.uniprot.org/enzyme/2.8.1.8 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/2.8.1.- |