http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.3.-.- |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.3.1.- |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/2000/01/rdf-schema#comment | "The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalyzed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A."xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/2000/01/rdf-schema#comment | "A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4 and EC 1.8.1.4."xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/2000/01/rdf-schema#comment | "In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine."xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/2004/02/skos/core#prefLabel | "dihydrolipoyllysine-residue (2-methylpropanoyl)transferase"xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/6746648 |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/773366 |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7913832 |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10966480 |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/2004/02/skos/core#altLabel | "dihydrolipoyl transacylase"xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/2.3.1.168#SIPFFE5CB49142130AA |
http://purl.uniprot.org/enzyme/2.3.1.168 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/2.3.1.- |
http://purl.uniprot.org/uniprot/A0A0B1TU62 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.168 |
http://purl.uniprot.org/uniprot/A0A085MM32 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.168 |
http://purl.uniprot.org/uniprot/A0A1Y5Q062 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.168 |
http://purl.uniprot.org/uniprot/O06159 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.168 |
http://purl.uniprot.org/uniprot/A0A3B0YQM1 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.168 |
http://purl.uniprot.org/uniprot/A6HV98 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.168 |
http://purl.uniprot.org/uniprot/A0A090QCK2 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.168 |
http://purl.uniprot.org/uniprot/P53395 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.168 |
http://purl.uniprot.org/uniprot/A0AA88Z8Q2 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.168 |