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An essentially pure preparation of the cobamide-dependent ribonucleotide reductase from Lactobacillus leichmannii can utilize the purified thioredoxin system from Escherichia coli B as hydrogen donor in place of dihydrolipoate in the reduction of the triphosphates of cytidine, guanosine, adenosine, and uridine. The substrate specificity pattern of L. leichmannii reductase is determined by ATP and various deoxyribonucleoside triphosphates, apparently acting as allosteric effectors.
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Beck et al. (1966) studied this question.
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