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http://purl.uniprot.org/enzyme/1.17.4.1http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.17.4.1http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.17.4.1http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.17.4.-
http://purl.uniprot.org/enzyme/1.17.4.1http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.17.-.-
http://purl.uniprot.org/enzyme/1.17.4.1http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.17.4.1http://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/1.17.4.1http://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/1.17.4.1http://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/1.17.4.1http://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/1.17.4.1http://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/1.17.4.1http://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/1.17.4.1http://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/1.17.4.1http://www.w3.org/2004/02/skos/core#prefLabel"ribonucleoside-diphosphate reductase"xsd:string
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16376858
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10430881
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/4543472
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/5330119
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/5330120
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/5926184
http://purl.uniprot.org/enzyme/1.17.4.1http://www.w3.org/2004/02/skos/core#altLabel"ribonucleotide reductase"xsd:string
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.17.4.1#SIP91132D47D571246F
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.17.4.1#SIP59C9FD34A69A4FEF
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.17.4.1#SIP5B9E8A2A1F01ADA3
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.17.4.1#SIPAA7F0F7290CAB928
http://purl.uniprot.org/enzyme/1.17.4.1http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.17.4.1#SIPAFD45215B7A89F15