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Ribonucleotide Reductases

Annual Review of Biochemistry, 2006
Ribonucleotide reductases (RNRs) transform RNA building blocks to DNA building blocks by catalyzing the substitution of the 2′OH-group of a ribonucleotide with a hydrogen by a mechanism involving protein radicals. Three classes of RNRs employ different mechanisms for the generation of the protein radical. Recent structural studies of members from each
Pär, Nordlund, Peter, Reichard
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Tinkering with a viral ribonucleotide reductase

Trends in Biochemical Sciences, 2009
Ribonucleotide reductase (RNR), a crucial enzyme for nucleotide anabolism, is encoded by all living organisms and by large DNA viruses such as the herpesviruses. Surprisingly, the beta-herpesvirus subfamily RNR R1 subunit homologues are catalytically inactive and their function remained enigmatic for many years.
LEMBO, David, Brune W.
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Ribonucleotide Reductase—a Radical Enzyme

Science, 1983
Ribonucleotide reductases catalyze the enzymatic formation of deoxyribonucleotides, an obligatory step in DNA synthesis. The native form of the enzyme from Escherichia coli or from mammalian sources contains as part of its polypeptide structure a free tyrosyl radical, stabilized by an iron center.
Peter Reichard, Anders Ehrenberg
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The interaction of adeninylalkycobalamins with ribonucleotide reductase

Biochimica et Biophysica Acta (BBA) - General Subjects, 1976
Several structural analogs of adenosylcobalamin, containing 2, 3, 4, 5 and 6 methylene carbons instead of the ribofuranose moiety, have been synthesized and their interaction with ribonucleotide reductase from Lactobacillus leichmannii has been investigated.
H.P.C. Hogenkamp   +2 more
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8-azidoadenosine and ribonucleotide reductase

Biochemical and Biophysical Research Communications, 1992
Inhibitors of ribonucleotide reductase are potential antiproliferative agents, since they deplete cells from DNA precursors. Substrate nucleoside analogues, carrying azido groups at the base moiety, are shown to have strong cytostatic properties, as measured by the inhibition of the incorporation of thymidine into DNA.
Marc Fontecave   +4 more
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Crystallographic investigations of ribonucleotide reductase

Biochemical Society Transactions, 1993
Introduction Ribonucleotide reductase catalyses the de novo production of deoxyribonucleotides. The enzyme reduces all the four main ribonucleotides to the corresponding deoxyribonucleotides. In higher organisms and in Eschmkhziz coli. this takes place at the diphosphate level I 1 1. Kibonucleotide reductase from E.
Anders Aberg   +3 more
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Structural features of ribonucleotide reductase

Proteins: Structure, Function, and Bioinformatics, 1986
AbstractHerpes simplex virus type 1 (HSV‐1) encodes a ribonucleotide reductase which comprises two polypeptides with sizes of 136,000 (RR1) and 38,000 mol. wt. (RR2). We have determined the entire DNA sequence specifying HSV‐1 RR1 and have identified two adjacent open reading frames in varicella‐zoster virus (VZV) which have homology to HSV RR1 and RR2;
I Nikas   +4 more
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Thiyl Radicals in Ribonucleotide Reductases

Science, 1996
The ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii catalyzes adenosylcobalamin (AdoCbl)-dependent nucleotide reduction, as well as exchange of the 5′ hydrogens of AdoCbl with solvent. A protein-based thiyl radical is proposed as an intermediate in both of these processes. In the presence
Stuart Licht   +2 more
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Drug action on ribonucleotide reductase

Advances in Enzyme Regulation, 1985
Ribonucleotide reductase catalyzes the rate-limiting step in DNA synthesis. It represents a key metabolic site at which specific inhibitors have been directed as potential antitumor agents. Several different classes of ribonucleotide reductase inhibitors have been generated and studied.
J G, Cory, G L, Carter
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Ribonucleotide reductases and radical reactions [PDF]

open access: possibleCellular and Molecular Life Sciences (CMLS), 1998
Ribonucleotide reductases (RNRs) catalyse the reduction of ribonucleotides to deoxyribonucleotides. They play a pivotal role in the regulation of DNA synthesis and are targets for antiproliferative drugs. Ribonucleotide reductases are unique enzymes in that they all require a protein radical for activity.
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