Partially purified ribonucleotide reductase from Saccharomyces cerevisiae was unstable in solution; however, enzyme activity could be maintained by quick-freezing and storage at low temperatures. The reduction of CDP was stimulated by ATP/Mg++, and maximal activity was obtained with E. coli thioredoxin as a reductant, but not with dithioerythritol. Enzyme activity was inhibited by dATP, hydroxyurea, and moderately high salt concentrations; addition of 5′-deoxyadenosylcobalamin or of iron salts was without effect. Gel filtration of the yeast extract yielded a fraction highly inhibitory to enzyme activity.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|