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anaerobic ribonucleoside-triphosphate reductase
glycine radical domain-containing protein
anaerobic ribonucleoside-triphosphate reductase, a class III ribonucleotide reductase, uses an oxygen-sensitive glycyl radical and an iron-sulfur cluster to catalyze the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides during anaerobic conditions
This model represents the oxygen-sensitive (anaerobic, class III) ribonucleotide reductase. The mechanism of the enzyme involves a glycine-centered radical [1], a C-terminal zinc binding site [2], and a set of conserved active site cysteines and asparagines [3]. This enzyme requires an activating component, NrdG, a radical-SAM domain containing enzyme (TIGR02491). Together the two form an alpha-2/beta-2 heterodimer.
anaerobic ribonucleoside triphosphate reductase
Catalyzes the reduction of nucleoside 5'-triphosphates to 2'-deoxynucleoside 5'-triphosphates
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