http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.8.1.- |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.8.-.- |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2000/01/rdf-schema#comment | "In vivo, the [2Fe-2S] cluster can be reassembled by the Isc or Suf iron-sulfur cluster assembly systems, to allow further catalysis."xsd:string |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2000/01/rdf-schema#comment | "In every reaction cycle, the enzyme consumes two molecules of AdoMet, each producing 5'-deoxyadenosine and 4,5-secobiotin."xsd:string |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2000/01/rdf-schema#comment | "Reaction with another equivalent of AdoMet results in abstraction of the C6 methylene pro-S hydrogen atom from 4,5-secobiotin, and the resulting carbon radical is quenched via formation of an intramolecular C-S bond, thus closing the biotin thiophane ring."xsd:string |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2000/01/rdf-schema#comment | "The sulfur donor is believed to be the [2Fe-2S] cluster, which is sacrificed in the process, so that in vitro the reaction is a single turnover."xsd:string |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster."xsd:string |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2004/02/skos/core#prefLabel | "biotin synthase"xsd:string |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8117110 |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2971595 |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/14704425 |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11444981 |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16042606 |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18690713 |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19821612 |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/2.8.1.6#SIP48101772A7884FFB |
http://purl.uniprot.org/enzyme/2.8.1.6 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/2.8.1.- |
http://purl.uniprot.org/uniprot/A0A923WJG8 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.8.1.6 |
http://purl.uniprot.org/uniprot/A0AA39L858 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.8.1.6 |
http://purl.uniprot.org/uniprot/A0AA97AHH7 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.8.1.6 |
http://purl.uniprot.org/uniprot/A0A9D8MFI9 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.8.1.6 |
http://purl.uniprot.org/uniprot/A0A0A8X7Q7 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.8.1.6 |