Ribonucleotide reductases: amazing and confusing.
نویسندگان
چکیده
منابع مشابه
Virus-Encoded Ribonucleotide Reductases
Ribonucleotide reductases [EC 1.17.4.] are a group of enzymes which critically contribute to the biosynthesis of deoxyribonucleotides (dNTPs), the monomeric precursors of DNA polymerization. By a radical reaction mechanism, they catalyze the reduction of the ribonucleotides, ADP, GDP, CDP, and UDP, mostly at the diphosphate level, to their deoxy conterparts dADP, dGDP, dCDP, and dUDP, respectiv...
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Ribonucleotide reductases catalyze in all living organisms the production of the deoxyribonucleotides required for DNA replication and repair. Their appearance during evolution was a prerequisite for the transition from the "RNA world," where RNA sufficed for both catalysis and information transfer, to today's situation where life depends on the interplay among DNA, RNA, and protein. Three clas...
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Ribonucleotide reductases catalyze a key step in DNA biosynthesis, using a diverse array of unprecedented metallo-cofactors to generate a transient protein radical that initiates nucleotide reduction. The new understanding of the chemistry and biochemistry of the system has allowed rational design of inhibitors of this process, which function as antitumor and antiviral agents.
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Ribonucleotide reductase (RNR) is a key enzyme that mediates the synthesis of deoxyribonucleotides, the DNA precursors, for DNA synthesis in every living cell. This enzyme converts ribonucleotides to deoxyribonucleotides, the building blocks for DNA replication, and repair. Clearly, RNR enzymes have contributed to the appearance of genetic material that exists today, being essential for the evo...
متن کاملAurintricarboxylic acid and polynucleotides as novel inhibitors of ribonucleotide reductases.
Ribonucleoside diphosphate reductases isolated from Escherichia coli, baker's yeast, Ehrlich ascites tumor cells, and unicellular green alga (Scenedesmus obliquus) are inhibited strongly and uniformly by the polymeric triphenylmethane dye, aurintricarboxylic acid. The molecule appears to interact simultaneously with the enzyme's various nucleotide and catalytic (iron-organic radical) sites. Oli...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)39357-3