The evolution of ribonucleotide reduction revisited.
Ribonucleotide reductases (RNRs) catalyze the conversion of both purine and pyrimidine nucleotides to deoxynucleotides in all organisms and provide all the monomeric precursors essential for both DNA replication and repair. RNRs have been divided into three classes on the basis of their unique metallo-cofactors. The exquisitely controlled free radical chemistry used by all RNRs, and the commonality of the structures of the subunits where the nucleotide reduction process occurs, together provide compelling evidence for the importance of chemistry in the divergent evolution of RNRs from a common progenitor.
Stubbe
J
J
Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave, Cambrige, MA 02139, USA. stubbe@mit.edu
Ge
J
J
Yee
C S
CS
D000495:Allosteric Site; D001665:Binding Sites; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology; D019143:Evolution, Molecular; D007778:Lactobacillus / Q000201:enzymology; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011770:Pyruvate Kinase / Q000737:chemistry; D012264:Ribonucleotide Reductases / Q000737:chemistry* / Q000145:classification* / Q000235:genetics*
D012264:Ribonucleotide Reductases; D011770:Pyruvate Kinase