http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.8.1.- |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.8.-.- |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#comment | "The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein."xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#comment | "In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups."xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#comment | "It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate."xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#comment | "Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine."xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#comment | "A component of the multienzyme 2-oxo-acid dehydrogenase complexes."xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#comment | "Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase."xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2000/01/rdf-schema#comment | "It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes."xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2004/02/skos/core#prefLabel | "dihydrolipoyl dehydrogenase"xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15642479 |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/13471525 |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/13767908 |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10966480 |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "dihydrolipoamide dehydrogenase"xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "L-protein"xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "lipoamide dehydrogenase (NADH)"xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "diaphorase"xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "E3 component of alpha-ketoacid dehydrogenase complexes"xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "LDP-Glc"xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "LDP-Val"xsd:string |
http://purl.uniprot.org/enzyme/1.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "dehydrolipoate dehydrogenase"xsd:string |