http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.3.-.- |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.3.1.- |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms."xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2000/01/rdf-schema#comment | "In the second step the acyl group is transferred to CoA."xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2000/01/rdf-schema#comment | "Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9."xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2000/01/rdf-schema#comment | "The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA."xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation."xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2004/02/skos/core#prefLabel | "acetyl-CoA C-acyltransferase"xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/13174544 |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2004/02/skos/core#altLabel | "3-ketoacyl-CoA thiolase"xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2004/02/skos/core#altLabel | "beta-ketothiolase"xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/2.3.1.16#SIPBB221B91485D667A |
http://purl.uniprot.org/enzyme/2.3.1.16 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/2.3.1.- |
http://purl.uniprot.org/uniprot/A0A9N9UPW0 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.16 |
http://purl.uniprot.org/uniprot/A0AA40DDH4 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.16 |
http://purl.uniprot.org/uniprot/A0A9E0IDJ3 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.16 |
http://purl.uniprot.org/uniprot/A0A8J5XZA3 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.16 |
http://purl.uniprot.org/uniprot/A0AA43QVQ1 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.16 |
http://purl.uniprot.org/uniprot/A0A8H6XE62 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.16 |
http://purl.uniprot.org/uniprot/A0A939EGA5 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.16 |
http://purl.uniprot.org/uniprot/A0A965CF71 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.16 |
http://purl.uniprot.org/uniprot/A0A9P5RJE1 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.3.1.16 |