http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.17.4.- |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.17.-.- |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#comment | "In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical."xsd:string |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#comment | "Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin."xsd:string |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#comment | "A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position."xsd:string |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#comment | "There are three types of this enzyme differing in their cofactors."xsd:string |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#comment | "This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair."xsd:string |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#comment | "The disulfide bridge is reduced by the action of thioredoxin. cf. EC 1.1.98.6 and EC 1.17.4.2."xsd:string |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2000/01/rdf-schema#comment | "The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues."xsd:string |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2004/02/skos/core#prefLabel | "ribonucleoside-diphosphate reductase"xsd:string |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16376858 |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10430881 |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/4543472 |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/5330119 |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/5330120 |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/5926184 |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://www.w3.org/2004/02/skos/core#altLabel | "ribonucleotide reductase"xsd:string |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.17.4.1#SIP91132D47D571246F |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.17.4.1#SIP59C9FD34A69A4FEF |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.17.4.1#SIP5B9E8A2A1F01ADA3 |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.17.4.1#SIPAA7F0F7290CAB928 |
http://purl.uniprot.org/enzyme/1.17.4.1 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.17.4.1#SIPAFD45215B7A89F15 |