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Ribonucleotide reductases.
TLDR
The X-ray structure of the class I Escherichia coli enzyme, including forms that bind substrate and allosteric effectors, confirms previous models of catalytic and allosterone mechanisms and suggests considerable mobility of the protein during catalysis. Expand
Interactions between deoxyribonucleotide and DNA synthesis.
  • P. Reichard
  • Biology, Medicine
  • Annual review of biochemistry
  • 1988
Ribonucleotide reductases.
TLDR
An intricate interplay between gene activation, enzyme inhibition, and protein degradation regulates, together with the allosteric effects, enzyme activity and provides the appropriate amount of deoxynucleotides for DNA replication and repair. Expand
Reduction of ribonucleotides.
TLDR
Structural Aspects and Reaction Mechanism; Regulation of Enzyme Synthesis; and Correlation o f I n Vitro and I n Vivo Activities. Expand
The deoxynucleotide triphosphohydrolase SAMHD1 is a major regulator of DNA precursor pools in mammalian cells
TLDR
In mammalian cells the cell cycle regulation of the two main enzymes controlling dNTP pool sizes is adjusted to the requirements of DNA replication. Expand
From RNA to DNA, why so many ribonucleotide reductases?
It is generally accepted that DNA appeared after RNA during the chemical evolution of life. To synthesize DNA, deoxyribonucleotides are required as building blocks. At present, these are formed fromExpand
ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. IV. ISOLATION AND CHARACTERIZATION OF THIOREDOXIN, THE HYDROGEN DONOR FROM ESCHERICHIA COLI B.
TLDR
The CDP-reductase system was purified from E. coli 13 a low molecular weight, heat-stable protein, hereafter called thioredoxin, and the requirement for reduced lipoate was replaced by either catalytic amounts of thiOREDoxin + TPNH or substrate amounts of chemically reduced dihydrothiored toxin. Expand
Role of effector binding in allosteric control of ribonucleoside diphosphate reductase.
TLDR
It appears that the l-sites are primarily involved in the regulation of the over-all activity of the enzyme, while binding of effectors to the h-sites influences the substrate-specificity of ribonucleoside diphosphate reductase. Expand
Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase
TLDR
The molecular mechanism of the allosteric substrate specificity regulation is revealed through the structures of a dimeric coenzyme B12–dependent RNR from Thermotoga maritima, both in complexes with four effector-substrate nucleotide pairs and in three complexes with only effector. Expand
NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase.
TLDR
It is proposed that its complementing activity during radical generation involves participation in the reduction of the ferric iron center of protein B2/HU, which is then linked to the reoxidation of iron by oxygen. Expand
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