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.
Interactions between deoxyribonucleotide and DNA synthesis.
- P. Reichard
- ChemistryAnnual Review of Biochemistry
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.
Reduction of ribonucleotides.
Structural Aspects and Reaction Mechanism; Regulation of Enzyme Synthesis; and Correlation o f I n Vitro and I n Vivo Activities.
The deoxynucleotide triphosphohydrolase SAMHD1 is a major regulator of DNA precursor pools in mammalian cells
- Elisa Franzolin, Giovanna Pontarin, V. Bianchi
- BiologyProceedings of the National Academy of Sciences
- 15 July 2013
In mammalian cells the cell cycle regulation of the two main enzymes controlling dNTP pool sizes is adjusted to the requirements of DNA replication.
From RNA to DNA, why so many ribonucleotide reductases?
- P. Reichard
- 18 June 1993
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 from…
Role of effector binding in allosteric control of ribonucleoside diphosphate reductase.
Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase
- K. Larsson, A. Jordan, R. Eliasson, P. Reichard, D. Logan, P. Nordlund
- Biology, ChemistryNature Structural &Molecular Biology
- 1 November 2004
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.
ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. IV. ISOLATION AND CHARACTERIZATION OF THIOREDOXIN, THE HYDROGEN DONOR FROM ESCHERICHIA COLI B.
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.