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http://purl.uniprot.org/enzyme/2.3.1.168http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.3.1.168http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.3.-.-
http://purl.uniprot.org/enzyme/2.3.1.168http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.3.1.-
http://purl.uniprot.org/enzyme/2.3.1.168http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.3.1.168http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.3.1.168http://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/2.3.1.168http://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/2.3.1.168http://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/2.3.1.168http://www.w3.org/2004/02/skos/core#prefLabel"dihydrolipoyllysine-residue (2-methylpropanoyl)transferase"xsd:string
http://purl.uniprot.org/enzyme/2.3.1.168http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6746648
http://purl.uniprot.org/enzyme/2.3.1.168http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/773366
http://purl.uniprot.org/enzyme/2.3.1.168http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7913832
http://purl.uniprot.org/enzyme/2.3.1.168http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10966480
http://purl.uniprot.org/enzyme/2.3.1.168http://www.w3.org/2004/02/skos/core#altLabel"dihydrolipoyl transacylase"xsd:string
http://purl.uniprot.org/enzyme/2.3.1.168http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.3.1.168#SIPFFE5CB49142130AA
http://purl.uniprot.org/enzyme/2.3.1.168http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/2.3.1.-
http://purl.uniprot.org/uniprot/A0A0B1TU62http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.168
http://purl.uniprot.org/uniprot/A0A085MM32http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.168
http://purl.uniprot.org/uniprot/A0A1Y5Q062http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.168
http://purl.uniprot.org/uniprot/O06159http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.168
http://purl.uniprot.org/uniprot/A0A3B0YQM1http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.168
http://purl.uniprot.org/uniprot/A6HV98http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.168
http://purl.uniprot.org/uniprot/A0A090QCK2http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.168
http://purl.uniprot.org/uniprot/P53395http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.168
http://purl.uniprot.org/uniprot/A0AA88Z8Q2http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.168