Hydrogen Donor Specificity of Cobamide-dependent Ribonucleotide Reductase and Allosteric Regulation of Substrate Specificity

作者：William S. Beck, Mehran Goulian, Agne Larsson, Peter A. Reichard · 发表于：Journal of Biological Chemistry · 年份：1966 · DOI：10.1016/s0021-9258(18)96683-4 · 被引用次数：42 · 研究领域：Metal-Catalyzed Oxygenation Mechanisms、Hemoglobin structure and function、Enzyme Structure and Function

Abstract 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.