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Recent crystallographic and biochemical studies have revealed the existence of numerous novel post-translational modifications within enzyme active sites. These modifications create structural and functional diversity. Although the function and biosynthesis of some of these modifications are well understood, others need further investigation.
Ribonucletide 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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